| anno_start anno_end anno_text entity_type sentence section |
| 0 17 Crystal structure evidence Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway TITLE |
| 21 26 SEL1L protein Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway TITLE |
| 54 57 SLR structure_element Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway TITLE |
| 0 5 SEL1L protein SEL1L, a component of the ERAD machinery, plays an important role in selecting and transporting ERAD substrates for degradation. ABSTRACT |
| 23 40 crystal structure evidence We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent). ABSTRACT |
| 48 53 mouse taxonomy_domain We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent). ABSTRACT |
| 54 59 SEL1L protein We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent). ABSTRACT |
| 60 74 central domain structure_element We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent). ABSTRACT |
| 91 108 Sel1-Like Repeats structure_element We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent). ABSTRACT |
| 110 127 SLR motifs 5 to 9 structure_element We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent). ABSTRACT |
| 146 155 SEL1Lcent structure_element We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent). ABSTRACT |
| 12 21 SEL1Lcent structure_element Strikingly, SEL1Lcent forms a homodimer with two-fold symmetry in a head-to-tail manner. ABSTRACT |
| 30 39 homodimer oligomeric_state Strikingly, SEL1Lcent forms a homodimer with two-fold symmetry in a head-to-tail manner. ABSTRACT |
| 68 80 head-to-tail protein_state Strikingly, SEL1Lcent forms a homodimer with two-fold symmetry in a head-to-tail manner. ABSTRACT |
| 18 29 SLR motif 9 structure_element Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface. ABSTRACT |
| 57 62 dimer oligomeric_state Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface. ABSTRACT |
| 87 101 domain-swapped protein_state Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface. ABSTRACT |
| 139 156 dimeric interface site Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface. ABSTRACT |
| 23 34 full-length protein_state We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells. ABSTRACT |
| 35 40 SEL1L protein We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells. ABSTRACT |
| 49 62 self-oligomer oligomeric_state We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells. ABSTRACT |
| 75 84 SEL1Lcent structure_element We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells. ABSTRACT |
| 95 104 mammalian taxonomy_domain We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells. ABSTRACT |
| 36 41 SLR-C structure_element Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1. ABSTRACT |
| 54 74 SLR motifs 10 and 11 structure_element Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1. ABSTRACT |
| 79 84 SEL1L protein Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1. ABSTRACT |
| 124 137 luminal loops structure_element Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1. ABSTRACT |
| 141 145 HRD1 protein Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1. ABSTRACT |
| 35 38 SLR structure_element Therefore, we propose that certain SLR motifs of SEL1L play a unique role in membrane bound ERAD machinery. ABSTRACT |
| 49 54 SEL1L protein Therefore, we propose that certain SLR motifs of SEL1L play a unique role in membrane bound ERAD machinery. ABSTRACT |
| 114 124 eukaryotes taxonomy_domain Protein quality control in the endoplasmic reticulum (ER) is essential for maintenance of cellular homeostasis in eukaryotes and is implicated in many severe diseases. INTRO |
| 105 122 polyubiquitinated protein_state Terminally misfolded proteins in the lumen or membrane of the ER are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome. INTRO |
| 144 154 proteasome complex_assembly Terminally misfolded proteins in the lumen or membrane of the ER are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome. INTRO |
| 70 79 conserved protein_state The process is called ER-associated protein degradation (ERAD) and is conserved in all eukaryotes. INTRO |
| 87 97 eukaryotes taxonomy_domain The process is called ER-associated protein degradation (ERAD) and is conserved in all eukaryotes. INTRO |
| 72 76 HRD1 protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 78 83 SEL1L protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 85 90 Hrd3p protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 93 109 Derlin-1, -2, -3 protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 111 116 Der1p protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 119 129 HERP-1, -2 protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 131 136 Usa1p protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 139 142 OS9 protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 144 148 Yos9 protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 151 156 XTP-B protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 162 167 Grp94 protein Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 258 263 yeast taxonomy_domain Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 268 277 metazoans taxonomy_domain Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans. INTRO |
| 0 5 Yeast taxonomy_domain Yeast ERAD components, which have been extensively characterized through genetic and biochemical studies, are comparable with mammalian ERAD components, sharing similar molecular functions and structural composition. INTRO |
| 73 104 genetic and biochemical studies experimental_method Yeast ERAD components, which have been extensively characterized through genetic and biochemical studies, are comparable with mammalian ERAD components, sharing similar molecular functions and structural composition. INTRO |
| 126 135 mammalian taxonomy_domain Yeast ERAD components, which have been extensively characterized through genetic and biochemical studies, are comparable with mammalian ERAD components, sharing similar molecular functions and structural composition. INTRO |
| 4 8 HRD1 protein The HRD1 E3 ubiquitin ligase, which is embedded in the ER membrane, is involved in translocating ERAD substrates across the ER membrane and catalyzing substrate ubiquitination via its cytosolic RING finger domain. INTRO |
| 9 28 E3 ubiquitin ligase protein_type The HRD1 E3 ubiquitin ligase, which is embedded in the ER membrane, is involved in translocating ERAD substrates across the ER membrane and catalyzing substrate ubiquitination via its cytosolic RING finger domain. INTRO |
| 194 212 RING finger domain structure_element The HRD1 E3 ubiquitin ligase, which is embedded in the ER membrane, is involved in translocating ERAD substrates across the ER membrane and catalyzing substrate ubiquitination via its cytosolic RING finger domain. INTRO |
| 0 5 SEL1L protein SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded. INTRO |
| 11 20 mammalian taxonomy_domain SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded. INTRO |
| 32 37 Hrd3p protein SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded. INTRO |
| 55 59 HRD1 protein SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded. INTRO |
| 70 74 HRD1 protein SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded. INTRO |
| 108 114 lectin protein_type SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded. INTRO |
| 115 118 OS9 protein SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded. INTRO |
| 15 20 SEL1L protein In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs). INTRO |
| 53 93 Class I major histocompatibility complex complex_assembly In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs). INTRO |
| 95 98 MHC complex_assembly In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs). INTRO |
| 100 112 heavy chains protein_type In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs). INTRO |
| 114 117 HCs protein_type In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs). INTRO |
| 39 44 Sel1l gene Recent research based on the inducible Sel1l knockout mouse model highlights the physiological functions of SEL1L. INTRO |
| 45 59 knockout mouse experimental_method Recent research based on the inducible Sel1l knockout mouse model highlights the physiological functions of SEL1L. INTRO |
| 108 113 SEL1L protein Recent research based on the inducible Sel1l knockout mouse model highlights the physiological functions of SEL1L. INTRO |
| 0 5 SEL1L protein SEL1L is required for ER homeostasis, which is essential for protein translation, pancreatic function, and cellular and organismal survival. INTRO |
| 46 51 SEL1L protein However, despite the functional importance of SEL1L, the molecular structure of SEL1L has not been solved. INTRO |
| 67 76 structure evidence However, despite the functional importance of SEL1L, the molecular structure of SEL1L has not been solved. INTRO |
| 80 85 SEL1L protein However, despite the functional importance of SEL1L, the molecular structure of SEL1L has not been solved. INTRO |
| 9 28 biochemical studies experimental_method Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs. INTRO |
| 41 46 SEL1L protein Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs. INTRO |
| 52 80 type I transmembrane protein protein_type Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs. INTRO |
| 97 111 luminal domain structure_element Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs. INTRO |
| 131 149 repeated Sel1-like structure_element Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs. INTRO |
| 151 154 SLR structure_element Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs. INTRO |
| 4 7 SLR structure_element The SLR motif is a structural motif that closely resembles the tetratricopeptide-repeat (TPR) motif, which is a protein-protein interaction module. INTRO |
| 63 87 tetratricopeptide-repeat structure_element The SLR motif is a structural motif that closely resembles the tetratricopeptide-repeat (TPR) motif, which is a protein-protein interaction module. INTRO |
| 89 92 TPR structure_element The SLR motif is a structural motif that closely resembles the tetratricopeptide-repeat (TPR) motif, which is a protein-protein interaction module. INTRO |
| 36 50 luminal domain structure_element Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level. INTRO |
| 54 59 SEL1L protein Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level. INTRO |
| 126 136 chaperones protein_type Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level. INTRO |
| 195 198 SLR structure_element Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level. INTRO |
| 251 261 HRD1-SEL1L complex_assembly Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level. INTRO |
| 262 271 E3 ligase protein_type Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level. INTRO |
| 28 31 SLR structure_element Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters. INTRO |
| 80 83 SLR structure_element Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters. INTRO |
| 94 99 SEL1L protein Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters. INTRO |
| 154 159 SEL1L protein Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters. INTRO |
| 203 217 luminal domain structure_element Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters. INTRO |
| 233 236 SLR structure_element Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters. INTRO |
| 64 69 SEL1L protein Therefore, the way in which these unique structural features of SEL1L are related to its critical function in ERAD remains to be elucidated. INTRO |
| 50 53 SLR structure_element To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L. INTRO |
| 65 70 SEL1L protein To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L. INTRO |
| 98 115 crystal structure evidence To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L. INTRO |
| 131 134 SLR structure_element To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L. INTRO |
| 145 150 SEL1L protein To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L. INTRO |
| 18 32 central domain structure_element We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9. INTRO |
| 36 41 SEL1L protein We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9. INTRO |
| 54 76 SLR motifs 5 through 9 structure_element We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9. INTRO |
| 78 87 SEL1Lcent structure_element We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9. INTRO |
| 104 109 dimer oligomeric_state We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9. INTRO |
| 163 174 SLR motif 9 structure_element We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9. INTRO |
| 19 24 SLR-C structure_element We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1. INTRO |
| 40 60 SLR motifs 10 and 11 structure_element We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1. INTRO |
| 101 113 luminal loop structure_element We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1. INTRO |
| 117 121 HRD1 protein We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1. INTRO |
| 60 63 SLR structure_element Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD. INTRO |
| 75 80 SEL1L protein Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD. INTRO |
| 112 118 stable protein_state Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD. INTRO |
| 119 128 oligomers oligomeric_state Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD. INTRO |
| 0 23 Structure Determination experimental_method Structure Determination of SEL1Lcent RESULTS |
| 27 36 SEL1Lcent structure_element Structure Determination of SEL1Lcent RESULTS |
| 4 16 Mus musculus species The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p. RESULTS |
| 17 22 SEL1L protein The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p. RESULTS |
| 93 98 yeast taxonomy_domain The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p. RESULTS |
| 108 113 Hrd3p protein The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p. RESULTS |
| 0 5 Mouse taxonomy_domain Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A). RESULTS |
| 6 11 SEL1L protein Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A). RESULTS |
| 23 49 fibronectin type II domain structure_element Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A). RESULTS |
| 84 87 SLR structure_element Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A). RESULTS |
| 108 128 transmembrane domain structure_element Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A). RESULTS |
| 7 10 SLR structure_element The 11 SLR motifs are located in the ER lumen and account for more than two thirds of the mass of full-length SEL1L. RESULTS |
| 98 109 full-length protein_state The 11 SLR motifs are located in the ER lumen and account for more than two thirds of the mass of full-length SEL1L. RESULTS |
| 110 115 SEL1L protein The 11 SLR motifs are located in the ER lumen and account for more than two thirds of the mass of full-length SEL1L. RESULTS |
| 4 7 SLR structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 72 88 linker sequences structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 109 112 SLR structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 121 126 SLR-N structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 128 145 SLR motifs 1 to 4 structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 148 153 SLR-M structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 155 172 SLR motifs 5 to 9 structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 179 184 SLR-C structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 186 205 SLR motifs 10 to 11 structure_element The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A). RESULTS |
| 0 18 Sequence alignment experimental_method Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 26 29 SLR structure_element Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 68 83 linker sequence structure_element Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 94 101 336–345 residue_range Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 111 116 SLR-N structure_element Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 121 126 SLR-M structure_element Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 138 153 linker sequence structure_element Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 164 171 528–635 residue_range Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 181 186 SLR-M structure_element Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 191 196 SLR-C structure_element Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A). RESULTS |
| 30 41 full-length protein_state We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria. RESULTS |
| 42 47 mouse taxonomy_domain We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria. RESULTS |
| 48 53 SEL1L protein We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria. RESULTS |
| 77 97 transmembrane domain structure_element We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria. RESULTS |
| 126 133 735–755 residue_range We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria. RESULTS |
| 139 161 expression in bacteria experimental_method We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria. RESULTS |
| 13 24 full-length protein_state However, the full-length SEL1L protein aggregated in solution and produced no soluble protein. RESULTS |
| 25 30 SEL1L protein However, the full-length SEL1L protein aggregated in solution and produced no soluble protein. RESULTS |
| 30 35 SEL1L protein To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species. RESULTS |
| 50 78 serial truncation constructs experimental_method To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species. RESULTS |
| 82 87 SEL1L protein To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species. RESULTS |
| 111 114 SLR structure_element To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species. RESULTS |
| 126 142 highly conserved protein_state To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species. RESULTS |
| 5 10 SLR-N structure_element Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography. RESULTS |
| 21 28 194–343 residue_range Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography. RESULTS |
| 34 39 SLR-C structure_element Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography. RESULTS |
| 50 57 639–719 residue_range Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography. RESULTS |
| 94 119 MBP tag at the N-terminus experimental_method Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography. RESULTS |
| 170 199 size-exclusion chromatography experimental_method Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography. RESULTS |
| 13 27 central region structure_element However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography. RESULTS |
| 31 36 SEL1L protein However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography. RESULTS |
| 58 65 337–554 residue_range However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography. RESULTS |
| 120 149 size-exclusion chromatography experimental_method However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography. RESULTS |
| 44 58 central region structure_element To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing. RESULTS |
| 62 67 SEL1L protein To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing. RESULTS |
| 72 105 digested the protein with trypsin experimental_method To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing. RESULTS |
| 147 155 SDS-PAGE experimental_method To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing. RESULTS |
| 160 181 N-terminal sequencing experimental_method To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing. RESULTS |
| 68 73 SEL1L protein The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A). RESULTS |
| 83 90 348–533 residue_range The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A). RESULTS |
| 92 101 SEL1Lcent structure_element The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A). RESULTS |
| 124 143 structural analysis experimental_method The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A). RESULTS |
| 0 8 Crystals evidence Crystals of SEL1Lcent grew in space group P21 with four copies of SEL1Lcent (a total of 82 kDa) in the asymmetric unit. RESULTS |
| 12 21 SEL1Lcent structure_element Crystals of SEL1Lcent grew in space group P21 with four copies of SEL1Lcent (a total of 82 kDa) in the asymmetric unit. RESULTS |
| 66 75 SEL1Lcent structure_element Crystals of SEL1Lcent grew in space group P21 with four copies of SEL1Lcent (a total of 82 kDa) in the asymmetric unit. RESULTS |
| 4 13 structure evidence The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods). RESULTS |
| 36 75 single-wavelength anomalous diffraction experimental_method The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods). RESULTS |
| 77 80 SAD experimental_method The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods). RESULTS |
| 95 103 selenium chemical The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods). RESULTS |
| 66 74 selenium chemical The assignment of residues during model building was aided by the selenium atom positions, and the structure was refined with native data to 2.6 Å resolution with Rwork/Rfree values of 20.7/27.7%. RESULTS |
| 99 108 structure evidence The assignment of residues during model building was aided by the selenium atom positions, and the structure was refined with native data to 2.6 Å resolution with Rwork/Rfree values of 20.7/27.7%. RESULTS |
| 163 174 Rwork/Rfree evidence The assignment of residues during model building was aided by the selenium atom positions, and the structure was refined with native data to 2.6 Å resolution with Rwork/Rfree values of 20.7/27.7%. RESULTS |
| 8 17 Structure evidence Overall Structure of SEL1Lcent RESULTS |
| 21 30 SEL1Lcent structure_element Overall Structure of SEL1Lcent RESULTS |
| 4 9 mouse taxonomy_domain The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1). RESULTS |
| 10 19 SEL1Lcent structure_element The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1). RESULTS |
| 20 32 crystallized experimental_method The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1). RESULTS |
| 38 47 homodimer oligomeric_state The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1). RESULTS |
| 68 78 homodimers oligomeric_state The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1). RESULTS |
| 8 17 SEL1Lcent structure_element The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B). RESULTS |
| 28 36 dimerize oligomeric_state The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B). RESULTS |
| 42 54 head-to-tail protein_state The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B). RESULTS |
| 72 99 two-fold symmetry interface site The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B). RESULTS |
| 134 143 structure evidence The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B). RESULTS |
| 14 23 structure evidence The resulting structure resembles the yin-yang symbol with overall dimensions of 60 × 60 × 25 Å, where a SEL1Lcent monomer corresponds to half the symbol. RESULTS |
| 105 114 SEL1Lcent structure_element The resulting structure resembles the yin-yang symbol with overall dimensions of 60 × 60 × 25 Å, where a SEL1Lcent monomer corresponds to half the symbol. RESULTS |
| 115 122 monomer oligomeric_state The resulting structure resembles the yin-yang symbol with overall dimensions of 60 × 60 × 25 Å, where a SEL1Lcent monomer corresponds to half the symbol. RESULTS |
| 4 9 dimer oligomeric_state The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms). RESULTS |
| 62 69 monomer oligomeric_state The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms). RESULTS |
| 114 123 protomers oligomeric_state The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms). RESULTS |
| 146 172 root mean square deviation evidence The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms). RESULTS |
| 174 178 RMSD evidence The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms). RESULTS |
| 5 13 protomer oligomeric_state Each protomer is composed of ten α-helices, which form the five SLRs, resulting in an elongated curved structure, confirming the primary structure prediction (Fig. 1D). RESULTS |
| 33 42 α-helices structure_element Each protomer is composed of ten α-helices, which form the five SLRs, resulting in an elongated curved structure, confirming the primary structure prediction (Fig. 1D). RESULTS |
| 64 68 SLRs structure_element Each protomer is composed of ten α-helices, which form the five SLRs, resulting in an elongated curved structure, confirming the primary structure prediction (Fig. 1D). RESULTS |
| 4 13 α-helices structure_element The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs. RESULTS |
| 28 37 structure evidence The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs. RESULTS |
| 55 56 A structure_element The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs. RESULTS |
| 61 62 B structure_element The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs. RESULTS |
| 88 92 TPRs structure_element The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs. RESULTS |
| 97 101 SLRs structure_element The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs. RESULTS |
| 0 15 Helices A and B structure_element Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D). RESULTS |
| 71 78 helices structure_element Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D). RESULTS |
| 104 108 turn structure_element Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D). RESULTS |
| 113 117 loop structure_element Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D). RESULTS |
| 22 26 loop structure_element In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR. RESULTS |
| 95 102 helix B structure_element In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR. RESULTS |
| 110 113 SLR structure_element In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR. RESULTS |
| 118 125 helix A structure_element In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR. RESULTS |
| 138 141 SLR structure_element In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR. RESULTS |
| 41 45 SLRs structure_element This arrangement is a unique feature for SLRs among the major classes of repeats containing an α-solenoid. RESULTS |
| 95 105 α-solenoid structure_element This arrangement is a unique feature for SLRs among the major classes of repeats containing an α-solenoid. RESULTS |
| 34 44 α-solenoid structure_element Starting from its N-terminus, the α-solenoid of SEL1L extends across a semi-circle in a right-handed superhelix fashion along the rotation axis of the yin-yang circle. RESULTS |
| 48 53 SEL1L protein Starting from its N-terminus, the α-solenoid of SEL1L extends across a semi-circle in a right-handed superhelix fashion along the rotation axis of the yin-yang circle. RESULTS |
| 151 166 yin-yang circle structure_element Starting from its N-terminus, the α-solenoid of SEL1L extends across a semi-circle in a right-handed superhelix fashion along the rotation axis of the yin-yang circle. RESULTS |
| 25 27 9B structure_element However, the last helix, 9B, at the C-terminus adopts a different conformation, lying parallel to the long axis of helix 9A instead of forming an antiparallel SLR. RESULTS |
| 115 123 helix 9A structure_element However, the last helix, 9B, at the C-terminus adopts a different conformation, lying parallel to the long axis of helix 9A instead of forming an antiparallel SLR. RESULTS |
| 159 162 SLR structure_element However, the last helix, 9B, at the C-terminus adopts a different conformation, lying parallel to the long axis of helix 9A instead of forming an antiparallel SLR. RESULTS |
| 28 36 helix 9B structure_element This unique conformation of helix 9B most likely contributes to formation of the dimer structure of SEL1Lcent, as detailed below. RESULTS |
| 81 86 dimer oligomeric_state This unique conformation of helix 9B most likely contributes to formation of the dimer structure of SEL1Lcent, as detailed below. RESULTS |
| 100 109 SEL1Lcent structure_element This unique conformation of helix 9B most likely contributes to formation of the dimer structure of SEL1Lcent, as detailed below. RESULTS |
| 31 34 SLR structure_element With the exception of the last SLR, the four α-helix pairs possess similar conformations, with RMSD values of 0.7 Å for all Cα atoms. RESULTS |
| 45 52 α-helix structure_element With the exception of the last SLR, the four α-helix pairs possess similar conformations, with RMSD values of 0.7 Å for all Cα atoms. RESULTS |
| 95 99 RMSD evidence With the exception of the last SLR, the four α-helix pairs possess similar conformations, with RMSD values of 0.7 Å for all Cα atoms. RESULTS |
| 41 60 pairwise alignments experimental_method Although the sequence similarity for the pairwise alignments varies between 25% and 35%, all the residues present in the SLR motifs are conserved among the five pairs. RESULTS |
| 121 124 SLR structure_element Although the sequence similarity for the pairwise alignments varies between 25% and 35%, all the residues present in the SLR motifs are conserved among the five pairs. RESULTS |
| 136 145 conserved protein_state Although the sequence similarity for the pairwise alignments varies between 25% and 35%, all the residues present in the SLR motifs are conserved among the five pairs. RESULTS |
| 4 7 SLR structure_element The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible. RESULTS |
| 18 23 SLR-M structure_element The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible. RESULTS |
| 40 43 524 residue_number The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible. RESULTS |
| 72 79 525–533 residue_range The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible. RESULTS |
| 118 138 electron density map evidence The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible. RESULTS |
| 171 186 highly flexible protein_state The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible. RESULTS |
| 31 36 dimer oligomeric_state Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit. RESULTS |
| 50 55 SEL1L protein Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit. RESULTS |
| 68 71 SLR structure_element Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit. RESULTS |
| 115 124 SEL1Lcent structure_element Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit. RESULTS |
| 125 130 dimer oligomeric_state Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit. RESULTS |
| 144 161 crystal structure evidence Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit. RESULTS |
| 10 22 cross-linked experimental_method First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 23 32 SEL1Lcent structure_element First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 58 63 SEL1L protein First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 65 74 SEL1Llong mutant First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 85 92 337–554 residue_range First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 126 140 glutaraldehyde chemical First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 142 144 GA chemical First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 149 170 dimethyl suberimidate chemical First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 172 175 DMS chemical First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 206 214 SDS-PAGE experimental_method First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE. RESULTS |
| 35 40 dimer oligomeric_state We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B). RESULTS |
| 50 59 SEL1Lcent structure_element We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B). RESULTS |
| 64 73 SEL1Llong mutant We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B). RESULTS |
| 79 91 cross-linked experimental_method We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B). RESULTS |
| 119 121 GA chemical We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B). RESULTS |
| 134 137 DMS chemical We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B). RESULTS |
| 19 49 analytical ultracentrifugation experimental_method Next, we conducted analytical ultracentrifugation of SEL1Lcent. RESULTS |
| 53 62 SEL1Lcent structure_element Next, we conducted analytical ultracentrifugation of SEL1Lcent. RESULTS |
| 20 33 cross-linking experimental_method Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C). RESULTS |
| 40 70 analytical ultracentrifugation experimental_method Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C). RESULTS |
| 89 105 molecular weight evidence Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C). RESULTS |
| 109 118 SEL1Lcent structure_element Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C). RESULTS |
| 136 141 dimer oligomeric_state Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C). RESULTS |
| 54 59 dimer oligomeric_state Taken together, these data indicate that some kind of dimer is formed in solution. RESULTS |
| 0 15 Dimer Interface site Dimer Interface of SEL1Lcent RESULTS |
| 19 28 SEL1Lcent structure_element Dimer Interface of SEL1Lcent RESULTS |
| 38 67 SLR motif containing proteins protein_type In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A). RESULTS |
| 82 90 monomers oligomeric_state In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A). RESULTS |
| 104 113 SEL1Lcent structure_element In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A). RESULTS |
| 132 166 two-fold homotypic dimer interface site In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A). RESULTS |
| 4 19 concave surface site The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement. RESULTS |
| 28 33 SEL1L protein The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement. RESULTS |
| 52 66 helix 5A to 9A structure_element The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement. RESULTS |
| 81 86 dimer oligomeric_state The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement. RESULTS |
| 64 73 protomers oligomeric_state However, no interactions were seen between the two-fold-related protomers through the concave inner surfaces themselves. RESULTS |
| 86 108 concave inner surfaces site However, no interactions were seen between the two-fold-related protomers through the concave inner surfaces themselves. RESULTS |
| 32 43 SLR motif 9 structure_element Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A). RESULTS |
| 81 83 9A structure_element Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A). RESULTS |
| 88 90 9B structure_element Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A). RESULTS |
| 134 149 concave surface site Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A). RESULTS |
| 176 198 dimerization interface site Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A). RESULTS |
| 0 8 Helix 9B structure_element Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation. RESULTS |
| 18 26 protomer oligomeric_state Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation. RESULTS |
| 74 88 concave region site Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation. RESULTS |
| 102 109 monomer oligomeric_state Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation. RESULTS |
| 121 135 domain-swapped protein_state Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation. RESULTS |
| 12 30 contact interfaces site Three major contact interfaces are involved in the interactions, and all interfaces are symmetrically related between the dimer subunits (Fig. 2A). RESULTS |
| 73 83 interfaces site Three major contact interfaces are involved in the interactions, and all interfaces are symmetrically related between the dimer subunits (Fig. 2A). RESULTS |
| 122 127 dimer oligomeric_state Three major contact interfaces are involved in the interactions, and all interfaces are symmetrically related between the dimer subunits (Fig. 2A). RESULTS |
| 0 34 Structure-based sequence alignment experimental_method Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E). RESULTS |
| 42 47 SEL1L protein Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E). RESULTS |
| 79 93 ConSurf server experimental_method Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E). RESULTS |
| 136 152 dimer interfaces site Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E). RESULTS |
| 158 174 highly conserved protein_state Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E). RESULTS |
| 185 190 SEL1L protein Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E). RESULTS |
| 7 15 helix 9B structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 24 33 SEL1Lcent structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 77 89 inner groove site First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 99 102 SLR structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 103 112 α-helices structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 114 116 5B structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 118 120 6B structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 122 124 7B structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 130 132 8B structure_element First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart. RESULTS |
| 8 17 interface site In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 19 26 Leu 516 residue_name_number In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 31 38 Tyr 519 residue_name_number In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 42 50 helix 9B structure_element In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 85 109 hydrophobic interactions bond_interaction In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 115 122 Trp 478 residue_name_number In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 126 134 helix 8B structure_element In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 136 143 Val 444 residue_name_number In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 147 155 helix 7B structure_element In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 157 164 Phe 411 residue_name_number In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 168 176 helix 6B structure_element In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 182 189 Leu 380 residue_name_number In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 193 201 helix 5B structure_element In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 211 220 SEL1Lcent structure_element In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 243 254 Interface 1 site In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail). RESULTS |
| 15 39 hydrophobic interactions bond_interaction In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 74 81 Tyr 519 residue_name_number In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 111 118 Ile 515 residue_name_number In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 124 131 H-bonds bond_interaction In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 157 166 conserved protein_state In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 167 174 Gln 377 residue_name_number In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 179 186 His 381 residue_name_number In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 190 198 helix 5B structure_element In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 223 231 protomer oligomeric_state In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer. RESULTS |
| 18 25 Gln 523 residue_name_number The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail). RESULTS |
| 35 41 H-bond bond_interaction The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail). RESULTS |
| 63 70 Asp 480 residue_name_number The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail). RESULTS |
| 95 103 protomer oligomeric_state The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail). RESULTS |
| 114 125 Interface 1 site The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail). RESULTS |
| 26 34 helix 9A structure_element Second, the residues from helix 9A interact with the residues from helix 5A of its counterpart in a head-to-tail orientation. RESULTS |
| 67 75 helix 5A structure_element Second, the residues from helix 9A interact with the residues from helix 5A of its counterpart in a head-to-tail orientation. RESULTS |
| 100 112 head-to-tail protein_state Second, the residues from helix 9A interact with the residues from helix 5A of its counterpart in a head-to-tail orientation. RESULTS |
| 8 17 interface site In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 47 55 helix 9A structure_element In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 67 74 Leu 503 residue_name_number In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 76 83 Tyr 499 residue_name_number In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 117 124 Lys 500 residue_name_number In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 155 177 van der Waals contacts bond_interaction In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 227 235 helix 5A structure_element In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 247 254 Tyr 360 residue_name_number In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 256 263 Leu 356 residue_name_number In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 265 272 Tyr 359 residue_name_number In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 278 285 Leu 363 residue_name_number In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363. RESULTS |
| 15 39 hydrophobic interactions bond_interaction In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 60 67 Asn 507 residue_name_number In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 72 79 Ser 510 residue_name_number In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 83 91 helix 9A structure_element In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 97 104 H-bonds bond_interaction In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 110 126 highly conserved protein_state In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 127 134 Arg 384 residue_name_number In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 142 146 loop structure_element In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 155 163 helix 5B structure_element In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 168 170 6A structure_element In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 197 205 protomer oligomeric_state In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail). RESULTS |
| 11 19 helix 9B structure_element Third, the helix 9B from each protomer is involved in the dimer interaction by forming a two-fold antiparallel symmetry. RESULTS |
| 30 38 protomer oligomeric_state Third, the helix 9B from each protomer is involved in the dimer interaction by forming a two-fold antiparallel symmetry. RESULTS |
| 58 63 dimer oligomeric_state Third, the helix 9B from each protomer is involved in the dimer interaction by forming a two-fold antiparallel symmetry. RESULTS |
| 66 73 Phe 518 residue_name_number In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail). RESULTS |
| 75 82 Leu 521 residue_name_number In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail). RESULTS |
| 88 95 Met 524 residue_name_number In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail). RESULTS |
| 195 206 Interface 3 site In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail). RESULTS |
| 56 73 crystal structure evidence To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 101 116 deletion mutant protein_state To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 118 130 SEL1L348–497 mutant To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 132 139 lacking protein_state To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 140 151 SLR motif 9 structure_element To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 153 161 helix 9A structure_element To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 166 168 9B structure_element To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 175 184 SEL1Lcent structure_element To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis. RESULTS |
| 4 19 deletion mutant protein_state The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 28 37 wild-type protein_state The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 38 47 SEL1Lcent structure_element The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 72 79 spectra evidence The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 83 98 CD spectroscopy experimental_method The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 120 128 deletion experimental_method The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 136 147 SLR motif 9 structure_element The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 190 199 SEL1Lcent structure_element The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3). RESULTS |
| 13 19 mutant protein_state However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C). RESULTS |
| 33 40 monomer oligomeric_state However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C). RESULTS |
| 44 73 size-exclusion chromatography experimental_method However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C). RESULTS |
| 78 108 analytical ultracentrifugation experimental_method However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C). RESULTS |
| 63 68 dimer oligomeric_state Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization. RESULTS |
| 95 114 triple point mutant protein_state Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization. RESULTS |
| 116 127 Interface 1 site Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization. RESULTS |
| 129 134 I515A mutant Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization. RESULTS |
| 136 141 L516A mutant Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization. RESULTS |
| 147 152 Y519A mutant Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization. RESULTS |
| 203 215 dimerization oligomeric_state Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization. RESULTS |
| 4 23 triple point mutant protein_state The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type. RESULTS |
| 38 45 monomer oligomeric_state The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type. RESULTS |
| 60 89 size-exclusion chromatography experimental_method The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type. RESULTS |
| 118 130 point mutant protein_state The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type. RESULTS |
| 132 137 Q460A mutant The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type. RESULTS |
| 174 183 wild-type protein_state The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type. RESULTS |
| 11 34 single-residue mutation experimental_method Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B). RESULTS |
| 36 41 L521A mutant Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B). RESULTS |
| 45 56 interface 3 site Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B). RESULTS |
| 58 84 abolished the dimerization protein_state Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B). RESULTS |
| 88 97 SEL1Lcent structure_element Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B). RESULTS |
| 0 7 Leu 521 residue_name_number Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer. RESULTS |
| 26 45 dimerization center site Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer. RESULTS |
| 66 76 9B helices structure_element Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer. RESULTS |
| 84 93 SEL1Lcent structure_element Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer. RESULTS |
| 94 99 dimer oligomeric_state Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer. RESULTS |
| 22 53 structural and biochemical data evidence Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface. RESULTS |
| 71 80 SEL1Lcent structure_element Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface. RESULTS |
| 93 98 dimer oligomeric_state Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface. RESULTS |
| 120 131 SLR motif 9 structure_element Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface. RESULTS |
| 135 144 SEL1Lcent structure_element Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface. RESULTS |
| 194 216 dimerization interface site Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface. RESULTS |
| 8 15 Glycine residue_name The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9 RESULTS |
| 26 30 G512 residue_name_number The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9 RESULTS |
| 35 39 G513 residue_name_number The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9 RESULTS |
| 50 55 Hinge structure_element The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9 RESULTS |
| 79 90 SLR Motif 9 structure_element The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9 RESULTS |
| 0 4 SLRs structure_element SLRs of mouse SEL1L were predicted using the TPRpred server. RESULTS |
| 8 13 mouse taxonomy_domain SLRs of mouse SEL1L were predicted using the TPRpred server. RESULTS |
| 14 19 SEL1L protein SLRs of mouse SEL1L were predicted using the TPRpred server. RESULTS |
| 45 59 TPRpred server experimental_method SLRs of mouse SEL1L were predicted using the TPRpred server. RESULTS |
| 25 36 full-length protein_state Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9. RESULTS |
| 37 42 SEL1L protein Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9. RESULTS |
| 66 69 SLR structure_element Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9. RESULTS |
| 111 133 SLR motifs 5 through 9 structure_element Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9. RESULTS |
| 35 43 helix 9A structure_element Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif. RESULTS |
| 48 50 9B structure_element Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif. RESULTS |
| 86 97 SLR repeats structure_element Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif. RESULTS |
| 118 129 SLR motif 9 structure_element Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif. RESULTS |
| 179 186 helices structure_element Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif. RESULTS |
| 230 233 SLR structure_element Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif. RESULTS |
| 17 34 crystal structure evidence According to our crystal structure, the central axis of helix 9B is almost parallel to that of helix 9A (Fig. 3B). RESULTS |
| 56 64 helix 9B structure_element According to our crystal structure, the central axis of helix 9B is almost parallel to that of helix 9A (Fig. 3B). RESULTS |
| 95 103 helix 9A structure_element According to our crystal structure, the central axis of helix 9B is almost parallel to that of helix 9A (Fig. 3B). RESULTS |
| 38 49 SLR motif 9 structure_element However, this unusual conformation of SLR motif 9 seems to be essential for dimer formation, as described earlier. RESULTS |
| 76 81 dimer oligomeric_state However, this unusual conformation of SLR motif 9 seems to be essential for dimer formation, as described earlier. RESULTS |
| 53 60 Gly 512 residue_name_number For this structural geometry, two adjacent residues, Gly 512 and Gly 513, in SEL1L confer flexibility at this position by adopting main-chain dihedral angles that are disallowed for non-glycine residues. RESULTS |
| 65 72 Gly 513 residue_name_number For this structural geometry, two adjacent residues, Gly 512 and Gly 513, in SEL1L confer flexibility at this position by adopting main-chain dihedral angles that are disallowed for non-glycine residues. RESULTS |
| 77 82 SEL1L protein For this structural geometry, two adjacent residues, Gly 512 and Gly 513, in SEL1L confer flexibility at this position by adopting main-chain dihedral angles that are disallowed for non-glycine residues. RESULTS |
| 47 54 Gly 512 residue_name_number The phi and psi dihedrals are 100° and 20° for Gly 512, and 110° and −20° for Gly 513, respectively (Fig. 3C). RESULTS |
| 78 85 Gly 513 residue_name_number The phi and psi dihedrals are 100° and 20° for Gly 512, and 110° and −20° for Gly 513, respectively (Fig. 3C). RESULTS |
| 0 7 Gly 513 residue_name_number Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A). RESULTS |
| 11 20 conserved protein_state Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A). RESULTS |
| 33 36 SLR structure_element Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A). RESULTS |
| 51 60 SEL1Lcent structure_element Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A). RESULTS |
| 66 73 Gly 512 residue_name_number Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A). RESULTS |
| 97 108 SLR motif 9 structure_element Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A). RESULTS |
| 112 121 SEL1Lcent structure_element Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A). RESULTS |
| 10 17 Gly-Gly structure_element Thus, the Gly-Gly residues generate an unusual sharp bend at the C-terminal SLR motif 9. RESULTS |
| 76 87 SLR motif 9 structure_element Thus, the Gly-Gly residues generate an unusual sharp bend at the C-terminal SLR motif 9. RESULTS |
| 21 28 glycine residue_name The involvement of a glycine residue in forming a hinge for domain swapping has been reported previously. RESULTS |
| 50 55 hinge structure_element The involvement of a glycine residue in forming a hinge for domain swapping has been reported previously. RESULTS |
| 20 27 Gly 513 residue_name_number The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p. RESULTS |
| 58 79 absolute conservation protein_state The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p. RESULTS |
| 119 132 budding yeast taxonomy_domain The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p. RESULTS |
| 141 146 Hrd3p protein The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p. RESULTS |
| 41 48 Gly 512 residue_name_number To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 53 60 Gly 513 residue_name_number To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 76 79 SLR structure_element To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 111 125 point mutation experimental_method To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 127 137 Gly to Ala mutant To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 186 193 Gly 512 residue_name_number To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 198 205 Gly 513 residue_name_number To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 241 249 helix 9B structure_element To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 267 275 protomer oligomeric_state To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 321 328 alanine residue_name To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 389 397 mutation experimental_method To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C). RESULTS |
| 34 42 mutation experimental_method This means that the effect of the mutation is mainly to generate a more restricted geometry at the hinge region. RESULTS |
| 99 104 hinge structure_element This means that the effect of the mutation is mainly to generate a more restricted geometry at the hinge region. RESULTS |
| 0 5 G512A mutant G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B. RESULTS |
| 9 14 G513A mutant G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B. RESULTS |
| 48 57 wild-type protein_state G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B. RESULTS |
| 74 103 size-exclusion chromatography experimental_method G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B. RESULTS |
| 174 181 glycine residue_name G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B. RESULTS |
| 248 256 helix 9B structure_element G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B. RESULTS |
| 13 26 double mutant protein_state However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 28 33 G512A mutant However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 34 39 G513A mutant However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 93 102 wild-type protein_state However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 120 128 mutation experimental_method However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 161 166 hinge structure_element However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 175 183 helix 9A structure_element However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 188 190 9B structure_element However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 230 238 helix 9B structure_element However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 325 334 SEL1Lcent structure_element However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6). RESULTS |
| 23 33 mutated to experimental_method When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 34 40 lysine residue_name When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 42 47 G512K mutant When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 48 53 G513K mutant When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 60 66 mutant protein_state When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 119 124 hinge structure_element When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 197 205 protomer oligomeric_state When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 209 218 SEL1Lcent structure_element When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 259 268 SEL1Lcent structure_element When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely. RESULTS |
| 4 9 G512K mutant The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D). RESULTS |
| 10 15 G513K mutant The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D). RESULTS |
| 16 29 double mutant protein_state The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D). RESULTS |
| 44 51 monomer oligomeric_state The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D). RESULTS |
| 64 93 size-exclusion chromatography experimental_method The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D). RESULTS |
| 61 69 mutation experimental_method A previous study shows that induction of steric hindrance by mutation destabilizes the dimerization interface of a different protein, ClC transporter. RESULTS |
| 87 109 dimerization interface site A previous study shows that induction of steric hindrance by mutation destabilizes the dimerization interface of a different protein, ClC transporter. RESULTS |
| 134 149 ClC transporter protein_type A previous study shows that induction of steric hindrance by mutation destabilizes the dimerization interface of a different protein, ClC transporter. RESULTS |
| 42 49 Gly 512 residue_name_number Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation. RESULTS |
| 54 61 Gly 513 residue_name_number Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation. RESULTS |
| 88 96 helix 9A structure_element Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation. RESULTS |
| 101 103 9B structure_element Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation. RESULTS |
| 139 153 domain-swapped protein_state Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation. RESULTS |
| 180 185 dimer oligomeric_state Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation. RESULTS |
| 0 5 SEL1L protein SEL1L Forms Self-oligomers through SEL1Lcent domain in vivo RESULTS |
| 12 26 Self-oligomers oligomeric_state SEL1L Forms Self-oligomers through SEL1Lcent domain in vivo RESULTS |
| 35 44 SEL1Lcent structure_element SEL1L Forms Self-oligomers through SEL1Lcent domain in vivo RESULTS |
| 21 26 SEL1L protein Next, we examined if SEL1L also forms self-oligomers in vivo using HEK293T cells. RESULTS |
| 38 52 self-oligomers oligomeric_state Next, we examined if SEL1L also forms self-oligomers in vivo using HEK293T cells. RESULTS |
| 13 24 full-length protein_state We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells. RESULTS |
| 25 30 SEL1L protein We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells. RESULTS |
| 31 33 HA experimental_method We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells. RESULTS |
| 38 43 SEL1L protein We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells. RESULTS |
| 44 48 FLAG experimental_method We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells. RESULTS |
| 49 66 fusion constructs experimental_method We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells. RESULTS |
| 71 85 co-transfected experimental_method We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells. RESULTS |
| 2 30 co-immunoprecipitation assay experimental_method A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A). RESULTS |
| 45 49 FLAG experimental_method A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A). RESULTS |
| 71 83 Western blot experimental_method A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A). RESULTS |
| 107 109 HA experimental_method A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A). RESULTS |
| 131 142 full-length protein_state A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A). RESULTS |
| 143 148 SEL1L protein A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A). RESULTS |
| 155 169 self-oligomers oligomeric_state A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A). RESULTS |
| 31 40 SEL1Lcent structure_element To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 90 101 full-length protein_state To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 102 107 SEL1L protein To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 122 131 SEL1Lcent structure_element To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 136 147 SLR motif 9 structure_element To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 148 156 deletion experimental_method To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 158 170 SEL1L348–497 mutant To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 194 202 fused to experimental_method To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 221 226 SEL1L protein To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 227 242 signal peptides structure_element To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides. RESULTS |
| 0 31 Co-immunoprecipitation analysis experimental_method Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A). RESULTS |
| 48 57 SEL1Lcent structure_element Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A). RESULTS |
| 105 116 full-length protein_state Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A). RESULTS |
| 117 122 SEL1L protein Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A). RESULTS |
| 130 142 SEL1L348–497 mutant Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A). RESULTS |
| 48 60 SEL1L348–497 mutant Interestingly, however, the expression level of SEL1L348–497 was consistently lower than that of SEL1Lcent (Fig. 4A,B). RESULTS |
| 97 106 SEL1Lcent structure_element Interestingly, however, the expression level of SEL1L348–497 was consistently lower than that of SEL1Lcent (Fig. 4A,B). RESULTS |
| 0 24 Semi-quantitative RT-PCR experimental_method Semi-quantitative RT-PCR revealed no significant difference in transcriptional levels of the two constructs (data not shown). RESULTS |
| 19 31 SEL1L348–497 mutant We speculated that SEL1L348–497 could be secreted while the SEL1Lcent is retained in the ER by association with the endogenous ERAD complex. RESULTS |
| 60 69 SEL1Lcent structure_element We speculated that SEL1L348–497 could be secreted while the SEL1Lcent is retained in the ER by association with the endogenous ERAD complex. RESULTS |
| 8 27 immunoprecipitation experimental_method Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B). RESULTS |
| 40 52 western blot experimental_method Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B). RESULTS |
| 105 117 SEL1L348–497 mutant Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B). RESULTS |
| 136 145 SEL1Lcent structure_element Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B). RESULTS |
| 35 47 SEL1L348–497 mutant We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment. RESULTS |
| 70 81 full-length protein_state We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment. RESULTS |
| 82 87 SEL1L protein We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment. RESULTS |
| 125 137 SEL1L348–497 mutant We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment. RESULTS |
| 166 175 SEL1Lcent structure_element We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment. RESULTS |
| 23 28 SEL1L protein In order to retain two SEL1L fragments in the ER lumen, we added KDEL ER retention sequence to the C-terminus of both fragments. RESULTS |
| 65 69 KDEL structure_element In order to retain two SEL1L fragments in the ER lumen, we added KDEL ER retention sequence to the C-terminus of both fragments. RESULTS |
| 70 91 ER retention sequence structure_element In order to retain two SEL1L fragments in the ER lumen, we added KDEL ER retention sequence to the C-terminus of both fragments. RESULTS |
| 24 28 KDEL structure_element Indeed, the addition of KDEL peptide increased the level of SEL1L348–497 in the ER lumen (Fig. 4D,E) and the immunostaining analysis showed both constructs were well localized to the ER (Fig. 4C). RESULTS |
| 60 72 SEL1L348–497 mutant Indeed, the addition of KDEL peptide increased the level of SEL1L348–497 in the ER lumen (Fig. 4D,E) and the immunostaining analysis showed both constructs were well localized to the ER (Fig. 4C). RESULTS |
| 109 123 immunostaining experimental_method Indeed, the addition of KDEL peptide increased the level of SEL1L348–497 in the ER lumen (Fig. 4D,E) and the immunostaining analysis showed both constructs were well localized to the ER (Fig. 4C). RESULTS |
| 28 37 SEL1Lcent structure_element We further analyzed whether SEL1Lcent may competitively inhibit the self-oligomerization of SEL1L in vivo. RESULTS |
| 92 97 SEL1L protein We further analyzed whether SEL1Lcent may competitively inhibit the self-oligomerization of SEL1L in vivo. RESULTS |
| 16 30 co-transfected experimental_method To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 50 56 tagged protein_state To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 57 68 full-length protein_state To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 69 74 SEL1L protein To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 76 81 SEL1L protein To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 82 84 HA experimental_method To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 89 94 SEL1L protein To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 95 99 FLAG experimental_method To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 105 121 increasing doses experimental_method To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 125 139 SEL1Lcent-KDEL mutant To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 141 158 SEL1L348–497-KDEL mutant To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 162 184 SEL1Lcent (L521A)-KDEL mutant To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively. RESULTS |
| 0 28 Co-immunoprecipitation assay experimental_method Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E). RESULTS |
| 43 52 wild-type protein_state Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E). RESULTS |
| 53 67 SEL1Lcent-KDEL mutant Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E). RESULTS |
| 129 140 full-length protein_state Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E). RESULTS |
| 13 30 SEL1L348–497-KDEL mutant In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F). RESULTS |
| 63 68 L521A mutant In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F). RESULTS |
| 72 81 SEL1Lcent structure_element In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F). RESULTS |
| 136 147 full-length protein_state In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F). RESULTS |
| 148 153 SEL1L protein In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F). RESULTS |
| 28 33 SEL1L protein These data suggest that the SEL1L forms self-oligomers and the oligomerization is mediated by the SEL1Lcent domain in vivo. RESULTS |
| 40 54 self-oligomers oligomeric_state These data suggest that the SEL1L forms self-oligomers and the oligomerization is mediated by the SEL1Lcent domain in vivo. RESULTS |
| 98 107 SEL1Lcent structure_element These data suggest that the SEL1L forms self-oligomers and the oligomerization is mediated by the SEL1Lcent domain in vivo. RESULTS |
| 0 21 Structural Comparison experimental_method Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins RESULTS |
| 25 30 SEL1L protein Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins RESULTS |
| 31 35 SLRs structure_element Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins RESULTS |
| 41 45 TPRs structure_element Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins RESULTS |
| 49 53 SLRs structure_element Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins RESULTS |
| 29 33 TPRs structure_element Previous studies reveal that TPRs and SLRs have similar consensus sequences, suggesting that their three-dimensional structures are also similar. RESULTS |
| 38 42 SLRs structure_element Previous studies reveal that TPRs and SLRs have similar consensus sequences, suggesting that their three-dimensional structures are also similar. RESULTS |
| 4 17 superposition experimental_method The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 30 34 TPRs structure_element The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 40 45 Cdc23 protein The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 47 55 S. pombe species The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 57 79 cell division cycle 23 protein The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 108 112 SLRs structure_element The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 118 122 HcpC protein The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 124 160 Helicobacter Cysteine-rich Protein C protein The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 184 189 RMSDs evidence The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar. RESULTS |
| 20 23 SLR structure_element This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 34 39 SEL1L protein This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 53 56 SLR structure_element This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 69 78 SEL1Lcent structure_element This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 91 111 structural alignment experimental_method This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 126 130 TPRs structure_element This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 132 136 RMSD evidence This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 167 172 Cdc23 protein This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 183 187 SLRs structure_element This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 189 193 RMSD evidence This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 224 228 HcpC protein This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A). RESULTS |
| 9 22 superimposing experimental_method However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 27 36 structure evidence However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 40 57 SLR motifs 5 to 9 structure_element However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 63 72 SEL1Lcent structure_element However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 90 95 Cdc23 protein However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 105 116 full-length protein_state However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 117 121 HcpC protein However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 122 132 structures evidence However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 147 164 SLR motifs 5 to 9 structure_element However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 168 177 SEL1Lcent structure_element However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 230 235 Cdc23 protein However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 239 243 HcpC protein However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 245 249 RMSD evidence However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B). RESULTS |
| 73 78 loops structure_element The differences may result from the differing numbers of residues in the loops and differences in antiparallel helix packing. RESULTS |
| 98 116 antiparallel helix structure_element The differences may result from the differing numbers of residues in the loops and differences in antiparallel helix packing. RESULTS |
| 20 29 conserved protein_state Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent. RESULTS |
| 30 45 disulfide bonds ptm Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent. RESULTS |
| 53 56 SLR structure_element Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent. RESULTS |
| 67 71 HcpC protein Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent. RESULTS |
| 76 80 HcpB protein Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent. RESULTS |
| 116 125 SEL1Lcent structure_element Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent. RESULTS |
| 79 82 SLR structure_element These factors contribute to the differences in the overall conformation of the SLR motifs in SEL1L and other SLR or TPR motif-containing proteins. RESULTS |
| 93 98 SEL1L protein These factors contribute to the differences in the overall conformation of the SLR motifs in SEL1L and other SLR or TPR motif-containing proteins. RESULTS |
| 109 145 SLR or TPR motif-containing proteins protein_type These factors contribute to the differences in the overall conformation of the SLR motifs in SEL1L and other SLR or TPR motif-containing proteins. RESULTS |
| 32 41 structure evidence Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins. RESULTS |
| 45 48 SLR structure_element Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins. RESULTS |
| 64 69 SEL1L protein Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins. RESULTS |
| 74 78 HcpC protein Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins. RESULTS |
| 4 7 TPR structure_element The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27. RESULTS |
| 33 45 dimerization oligomeric_state The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27. RESULTS |
| 66 71 Cdc23 protein The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27. RESULTS |
| 73 78 Cdc16 protein The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27. RESULTS |
| 84 89 Cdc27 protein The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27. RESULTS |
| 40 45 Cdc23 protein In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent. RESULTS |
| 47 52 Cdc23 protein In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent. RESULTS |
| 66 69 TPR structure_element In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent. RESULTS |
| 112 115 SLR structure_element In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent. RESULTS |
| 125 134 SEL1Lcent structure_element In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent. RESULTS |
| 10 13 TPR structure_element The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C). RESULTS |
| 24 29 Cdc23 protein The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C). RESULTS |
| 57 79 superhelical structure structure_element The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C). RESULTS |
| 128 133 dimer oligomeric_state The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C). RESULTS |
| 4 15 TPR motif 1 structure_element The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions. RESULTS |
| 17 21 TPR1 structure_element The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions. RESULTS |
| 31 36 Cdc23 protein The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions. RESULTS |
| 146 158 inner groove site The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions. RESULTS |
| 159 162 TPR structure_element The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions. RESULTS |
| 163 172 α-helices structure_element The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions. RESULTS |
| 17 26 structure evidence However, in this structure, a conformational change in the TPR motif itself is not observed. RESULTS |
| 59 62 TPR structure_element However, in this structure, a conformational change in the TPR motif itself is not observed. RESULTS |
| 20 24 HcpC protein Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent. RESULTS |
| 64 78 domain-swapped protein_state Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent. RESULTS |
| 96 99 SLR structure_element Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent. RESULTS |
| 110 114 HcpC protein Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent. RESULTS |
| 148 157 SEL1Lcent structure_element Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent. RESULTS |
| 9 14 SEL1L protein Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A). RESULTS |
| 36 39 SLR structure_element Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A). RESULTS |
| 61 65 HcpC protein Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A). RESULTS |
| 71 74 SLR structure_element Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A). RESULTS |
| 85 90 SEL1L protein Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A). RESULTS |
| 140 143 SLR structure_element Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A). RESULTS |
| 16 19 SLR structure_element The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B). RESULTS |
| 47 59 dimerization oligomeric_state The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B). RESULTS |
| 63 72 SEL1Lcent structure_element The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B). RESULTS |
| 82 85 SLR structure_element The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B). RESULTS |
| 126 152 semicircle of the yin-yang structure_element The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B). RESULTS |
| 0 8 Helix 5A structure_element Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L. RESULTS |
| 14 25 SLR motif 5 structure_element Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L. RESULTS |
| 32 40 helix 9A structure_element Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L. RESULTS |
| 46 57 SLR motif 9 structure_element Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L. RESULTS |
| 77 82 SEL1L protein Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L. RESULTS |
| 7 24 SLR motifs 5 to 9 structure_element If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L. RESULTS |
| 54 57 SLR structure_element If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L. RESULTS |
| 104 116 dimerization oligomeric_state If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L. RESULTS |
| 120 125 SEL1L protein If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L. RESULTS |
| 44 48 TPRs structure_element This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem. RESULTS |
| 52 57 Cdc23 protein This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem. RESULTS |
| 71 75 SLRs structure_element This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem. RESULTS |
| 79 83 HcpC protein This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem. RESULTS |
| 0 3 TPR structure_element TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein. RESULTS |
| 8 11 SLR structure_element TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein. RESULTS |
| 112 115 SLR structure_element TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein. RESULTS |
| 126 131 SEL1L protein TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein. RESULTS |
| 0 5 SLR-C structure_element SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop RESULTS |
| 9 14 SEL1L protein SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop RESULTS |
| 21 25 HRD1 protein SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop RESULTS |
| 37 49 Luminal Loop structure_element SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop RESULTS |
| 13 28 structural data evidence Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C. RESULTS |
| 112 119 mammals taxonomy_domain Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C. RESULTS |
| 161 164 SLR structure_element Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C. RESULTS |
| 176 181 SEL1L protein Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C. RESULTS |
| 27 30 SLR structure_element We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data. RESULTS |
| 59 71 dimerization oligomeric_state We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data. RESULTS |
| 75 80 SEL1L protein We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data. RESULTS |
| 94 111 crystal structure evidence We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data. RESULTS |
| 0 5 SLR-C structure_element SLR-C, which contains SLR motifs 10 to 11, might be involved in the interaction with HRD1. RESULTS |
| 22 41 SLR motifs 10 to 11 structure_element SLR-C, which contains SLR motifs 10 to 11, might be involved in the interaction with HRD1. RESULTS |
| 85 89 HRD1 protein SLR-C, which contains SLR motifs 10 to 11, might be involved in the interaction with HRD1. RESULTS |
| 34 39 yeast taxonomy_domain Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops. RESULTS |
| 96 101 Hrd3p protein Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops. RESULTS |
| 125 132 664–695 residue_range Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops. RESULTS |
| 158 162 Hrd1 protein Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops. RESULTS |
| 163 176 luminal loops structure_element Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops. RESULTS |
| 4 9 Hrd3p protein The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 19 26 664–695 residue_range The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 41 46 mouse taxonomy_domain The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 47 52 SEL1L protein The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 62 69 696–727 residue_range The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 96 105 helix 11B structure_element The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 115 122 697–709 residue_range The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 127 139 SLR motif 11 structure_element The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 146 160 well-conserved protein_state The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4). RESULTS |
| 76 94 SLR motif 10 to 11 structure_element This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 123 159 structure-guided SLR motif alignment experimental_method This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 182 197 structure study experimental_method This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 227 248 sequence conservation protein_state This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 257 266 mammalian taxonomy_domain This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 267 272 SEL1L protein This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 277 282 yeast taxonomy_domain This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 283 288 Hrd3p protein This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 296 315 SLR motifs 10 to 11 structure_element This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 352 356 HRD1 protein This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 358 363 Hrd1p protein This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5). RESULTS |
| 60 65 mouse taxonomy_domain To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L. RESULTS |
| 66 70 HRD1 protein To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L. RESULTS |
| 89 101 fused to GST experimental_method To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L. RESULTS |
| 164 167 SLR structure_element To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L. RESULTS |
| 178 183 SEL1L protein To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L. RESULTS |
| 94 99 SLR-N structure_element The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A). RESULTS |
| 101 106 SLR-M structure_element The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A). RESULTS |
| 108 113 SLR-C structure_element The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A). RESULTS |
| 119 126 monomer oligomeric_state The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A). RESULTS |
| 135 140 SLR-M structure_element The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A). RESULTS |
| 142 152 SLR-ML521A mutant The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A). RESULTS |
| 25 30 SLR-C structure_element Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1. RESULTS |
| 46 66 SLR motifs 10 and 11 structure_element Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1. RESULTS |
| 106 118 luminal loop structure_element Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1. RESULTS |
| 129 134 21–42 residue_range Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1. RESULTS |
| 139 143 HRD1 protein Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1. RESULTS |
| 27 32 SLR-N structure_element The molecular functions of SLR-N are unclear. RESULTS |
| 24 29 SLR-N structure_element One possibility is that SLR-N contributes to substrate recognition of proteins to be degraded because there are a couple of putative glycosylation sites within the SLR-N domain (Fig. 1A). RESULTS |
| 133 152 glycosylation sites site One possibility is that SLR-N contributes to substrate recognition of proteins to be degraded because there are a couple of putative glycosylation sites within the SLR-N domain (Fig. 1A). RESULTS |
| 164 169 SLR-N structure_element One possibility is that SLR-N contributes to substrate recognition of proteins to be degraded because there are a couple of putative glycosylation sites within the SLR-N domain (Fig. 1A). RESULTS |
| 0 9 SEL1Lcent structure_element SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C). RESULTS |
| 30 50 N-glycosylation site site SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C). RESULTS |
| 52 59 Asn 427 residue_name_number SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C). RESULTS |
| 70 86 highly conserved protein_state SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C). RESULTS |
| 158 163 SEL1L protein SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C). RESULTS |
| 164 169 dimer oligomeric_state SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C). RESULTS |
| 187 204 crystal structure evidence SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C). RESULTS |
| 72 77 yeast taxonomy_domain Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components. DISCUSS |
| 87 92 Hrd1p protein Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components. DISCUSS |
| 94 99 Der1p protein Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components. DISCUSS |
| 105 110 Usa1p protein Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components. DISCUSS |
| 4 9 Hrd1p protein The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography. DISCUSS |
| 24 30 dimers oligomeric_state The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography. DISCUSS |
| 36 66 sucrose gradient sedimentation experimental_method The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography. DISCUSS |
| 71 100 size-exclusion chromatography experimental_method The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography. DISCUSS |
| 24 41 HA-epitope-tagged protein_state Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 42 47 Hrd3p protein Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 51 56 Hrd1p protein Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 89 99 unmodified protein_state Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 100 105 Hrd3p protein Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 110 115 Hrd1p protein Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 152 157 Hrd1p protein Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 162 167 Hrd3p protein Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 168 178 homodimers oligomeric_state Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 219 222 Hrd complex_assembly Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex. DISCUSS |
| 100 105 yeast taxonomy_domain Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers. DISCUSS |
| 110 117 mammals taxonomy_domain Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers. DISCUSS |
| 139 148 mammalian taxonomy_domain Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers. DISCUSS |
| 192 201 oligomers oligomeric_state Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers. DISCUSS |
| 32 50 cross-linking data experimental_method This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer. DISCUSS |
| 67 72 human species This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer. DISCUSS |
| 73 77 HRD1 protein This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer. DISCUSS |
| 86 95 homodimer oligomeric_state This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer. DISCUSS |
| 39 56 crystal structure evidence Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9. DISCUSS |
| 61 77 biochemical data evidence Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9. DISCUSS |
| 95 100 mouse taxonomy_domain Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9. DISCUSS |
| 101 110 SEL1Lcent structure_element Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9. DISCUSS |
| 123 132 homodimer oligomeric_state Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9. DISCUSS |
| 172 183 SLR motif 9 structure_element Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9. DISCUSS |
| 63 68 dimer oligomeric_state We need to further test whether there are contacts involved in dimer formation in SEL1L in addition to those in the SLR-M region. DISCUSS |
| 82 87 SEL1L protein We need to further test whether there are contacts involved in dimer formation in SEL1L in addition to those in the SLR-M region. DISCUSS |
| 116 121 SLR-M structure_element We need to further test whether there are contacts involved in dimer formation in SEL1L in addition to those in the SLR-M region. DISCUSS |
| 3 8 yeast taxonomy_domain In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity. DISCUSS |
| 10 15 Usa1p protein In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity. DISCUSS |
| 39 44 Hrd1p protein In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity. DISCUSS |
| 49 54 Der1p protein In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity. DISCUSS |
| 83 88 Usa1p protein In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity. DISCUSS |
| 137 142 Hrd1p protein In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity. DISCUSS |
| 187 192 Hrd1p protein In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity. DISCUSS |
| 9 18 metazoans taxonomy_domain However, metazoans lack a clear Usa1p homolog. DISCUSS |
| 32 37 Usa1p protein However, metazoans lack a clear Usa1p homolog. DISCUSS |
| 9 18 mammalian taxonomy_domain Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p. DISCUSS |
| 19 23 HERP protein_type Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p. DISCUSS |
| 59 71 conserved in protein_state Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p. DISCUSS |
| 72 77 Usa1p protein Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p. DISCUSS |
| 105 109 HERP protein_type Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p. DISCUSS |
| 144 149 Usa1p protein Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p. DISCUSS |
| 37 58 transiently expressed protein_state Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 59 69 HRD1-SEL1L complex_assembly Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 109 116 lectins protein_type Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 117 120 OS9 protein Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 124 129 XTP-B protein Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 229 257 α-antitrypsin null Hong-Kong protein Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 259 262 NHK protein Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 281 288 NHK-QQQ mutant Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 296 301 lacks protein_state Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 306 327 N-glycosylation sites site Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites. DISCUSS |
| 117 126 homodimer oligomeric_state Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1. DISCUSS |
| 140 145 SEL1L protein Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1. DISCUSS |
| 199 202 HRD complex_assembly Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1. DISCUSS |
| 223 228 SEL1L protein Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1. DISCUSS |
| 252 264 complex with protein_state Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1. DISCUSS |
| 265 269 HRD1 protein Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1. DISCUSS |
| 55 60 SLR-C structure_element This is further supported by our data showing that the SLR-C of SEL1L directly interacts with the luminal fragment of HRD1 in the ER lumen. DISCUSS |
| 64 69 SEL1L protein This is further supported by our data showing that the SLR-C of SEL1L directly interacts with the luminal fragment of HRD1 in the ER lumen. DISCUSS |
| 118 122 HRD1 protein This is further supported by our data showing that the SLR-C of SEL1L directly interacts with the luminal fragment of HRD1 in the ER lumen. DISCUSS |
| 44 47 HRD complex_assembly Although the organization of membrane-bound HRD complex components may be very similar between metazoans and yeast, the molecular details of interactions between the components may not necessarily be conserved. DISCUSS |
| 95 104 metazoans taxonomy_domain Although the organization of membrane-bound HRD complex components may be very similar between metazoans and yeast, the molecular details of interactions between the components may not necessarily be conserved. DISCUSS |
| 109 114 yeast taxonomy_domain Although the organization of membrane-bound HRD complex components may be very similar between metazoans and yeast, the molecular details of interactions between the components may not necessarily be conserved. DISCUSS |
| 3 8 yeast taxonomy_domain In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L. DISCUSS |
| 52 57 Hrd3p protein In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L. DISCUSS |
| 68 71 SLR structure_element In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L. DISCUSS |
| 103 108 Hrd3p protein In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L. DISCUSS |
| 143 146 SLR structure_element In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L. DISCUSS |
| 157 162 SEL1L protein In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L. DISCUSS |
| 58 63 Hrd3p protein Furthermore, we are uncertain whether self-association of Hrd3p contributes to formation of the active form of the Hrd1p complex. DISCUSS |
| 96 102 active protein_state Furthermore, we are uncertain whether self-association of Hrd3p contributes to formation of the active form of the Hrd1p complex. DISCUSS |
| 115 120 Hrd1p protein Furthermore, we are uncertain whether self-association of Hrd3p contributes to formation of the active form of the Hrd1p complex. DISCUSS |
| 12 21 truncated protein_state Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex. DISCUSS |
| 33 37 Yos9 protein Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex. DISCUSS |
| 58 63 dimer oligomeric_state Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex. DISCUSS |
| 105 112 dimeric oligomeric_state Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex. DISCUSS |
| 126 131 Hrd1p protein Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex. DISCUSS |
| 49 53 Yos9 protein This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9. DISCUSS |
| 54 58 Yos9 protein This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9. DISCUSS |
| 93 124 immunoprecipitation experiments experimental_method This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9. DISCUSS |
| 130 135 yeast taxonomy_domain This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9. DISCUSS |
| 171 185 epitope-tagged protein_state This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9. DISCUSS |
| 198 202 Yos9 protein This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9. DISCUSS |
| 13 25 dimerization oligomeric_state However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer. DISCUSS |
| 29 33 Yos9 protein However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer. DISCUSS |
| 75 80 Hrd1p protein However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer. DISCUSS |
| 89 97 oligomer oligomeric_state However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer. DISCUSS |
| 14 26 dimerization oligomeric_state Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex. DISCUSS |
| 30 35 SEL1L protein Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex. DISCUSS |
| 68 77 mammalian taxonomy_domain Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex. DISCUSS |
| 78 81 HRD complex_assembly Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex. DISCUSS |
| 82 90 oligomer oligomeric_state Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex. DISCUSS |
| 64 69 SEL1L protein Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex. DISCUSS |
| 71 76 Hrd3p protein Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex. DISCUSS |
| 78 90 dimerization oligomeric_state Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex. DISCUSS |
| 144 147 HRD complex_assembly Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex. DISCUSS |
| 62 65 HRD complex_assembly Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 106 115 oligomers oligomeric_state Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 157 162 SEL1L protein Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 198 204 active protein_state Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 218 221 HRD complex_assembly Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 243 253 absence of protein_state Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 254 259 Usa1p protein Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 264 273 metazoans taxonomy_domain Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans. DISCUSS |
| 109 112 HRD complex_assembly These findings should provide a foundation for molecular-level studies to understand the membrane-associated HRD complex assembly in ERAD. DISCUSS |
| 0 17 Crystal Structure evidence Crystal Structure of SEL1Lcent. FIG |
| 21 30 SEL1Lcent structure_element Crystal Structure of SEL1Lcent. FIG |
| 46 58 Mus musculus species (A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis. FIG |
| 59 64 SEL1L protein (A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis. FIG |
| 80 99 proteolytic mapping experimental_method (A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis. FIG |
| 104 131 sequence/structure analysis experimental_method (A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis. FIG |
| 7 10 SLR structure_element The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs. FIG |
| 50 55 SLR-N structure_element The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs. FIG |
| 57 62 SLR-M structure_element The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs. FIG |
| 68 73 SLR-C structure_element The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs. FIG |
| 98 114 linker sequences structure_element The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs. FIG |
| 138 141 SLR structure_element The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs. FIG |
| 9 30 N-glycosylation sites site Putative N-glycosylation sites are indicated by black triangles. FIG |
| 18 35 crystal structure evidence We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis. FIG |
| 43 48 SLR-M structure_element We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis. FIG |
| 59 66 348–533 residue_range We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis. FIG |
| 117 126 SEL1Lcent structure_element We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis. FIG |
| 4 21 crystal structure evidence The crystal structure was determined by SAD phasing using selenium as the anomalous scatterer and refined to 2.6 Å resolution (Table 1). FIG |
| 40 51 SAD phasing experimental_method The crystal structure was determined by SAD phasing using selenium as the anomalous scatterer and refined to 2.6 Å resolution (Table 1). FIG |
| 58 66 selenium chemical The crystal structure was determined by SAD phasing using selenium as the anomalous scatterer and refined to 2.6 Å resolution (Table 1). FIG |
| 4 13 SEL1Lcent structure_element (C) SEL1Lcent ribbon diagram rotated 90° around a horizontal axis relative to (B). FIG |
| 8 16 protomer oligomeric_state (D) One protomer of the SEL1Lcent dimer. FIG |
| 24 33 SEL1Lcent structure_element (D) One protomer of the SEL1Lcent dimer. FIG |
| 34 39 dimer oligomeric_state (D) One protomer of the SEL1Lcent dimer. FIG |
| 30 39 SEL1Lcent structure_element Starting from the N-terminus, SEL1Lcent has five SLR motifs comprising ten α helices. FIG |
| 49 52 SLR structure_element Starting from the N-terminus, SEL1Lcent has five SLR motifs comprising ten α helices. FIG |
| 75 84 α helices structure_element Starting from the N-terminus, SEL1Lcent has five SLR motifs comprising ten α helices. FIG |
| 5 8 SLR structure_element Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences. FIG |
| 117 126 SEL1Lcent structure_element Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences. FIG |
| 145 152 ConSurf experimental_method Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences. FIG |
| 161 186 structure-based alignment experimental_method Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences. FIG |
| 194 199 SEL1L protein Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences. FIG |
| 102 107 SEL1L protein The surface is colored from red (high) to white (poor) according to the degree of conservation in the SEL1L phylogenetic orthologs. FIG |
| 38 46 protomer oligomeric_state The ribbon diagram of the counterpart protomer is drawn to show the orientation of the SEL1Lcent dimer. FIG |
| 87 96 SEL1Lcent structure_element The ribbon diagram of the counterpart protomer is drawn to show the orientation of the SEL1Lcent dimer. FIG |
| 97 102 dimer oligomeric_state The ribbon diagram of the counterpart protomer is drawn to show the orientation of the SEL1Lcent dimer. FIG |
| 0 15 Dimer Interface site Dimer Interface of SEL1Lcent. FIG |
| 19 28 SEL1Lcent structure_element Dimer Interface of SEL1Lcent. FIG |
| 38 47 SEL1Lcent structure_element (A) The diagram on the left shows the SEL1Lcent dimer viewed along the two-fold symmetry axis. FIG |
| 48 53 dimer oligomeric_state (A) The diagram on the left shows the SEL1Lcent dimer viewed along the two-fold symmetry axis. FIG |
| 15 30 contact regions site Three distinct contact regions are indicated with labeled boxes. FIG |
| 53 62 SEL1Lcent structure_element The close-up view on the right shows the residues of SEL1Lcent that contribute to dimer formation via the three contact interfaces. FIG |
| 82 87 dimer oligomeric_state The close-up view on the right shows the residues of SEL1Lcent that contribute to dimer formation via the three contact interfaces. FIG |
| 112 130 contact interfaces site The close-up view on the right shows the residues of SEL1Lcent that contribute to dimer formation via the three contact interfaces. FIG |
| 48 62 hydrogen bonds bond_interaction The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 75 84 protomers oligomeric_state The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 88 97 SEL1Lcent structure_element The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 103 132 Size-exclusion chromatography experimental_method The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 134 137 SEC experimental_method The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 155 164 wild-type protein_state The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 169 186 dimeric interface site The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 187 196 SEL1Lcent structure_element The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 197 204 mutants protein_state The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins. FIG |
| 38 41 SEC experimental_method The standard molecular masses for the SEC experiments (top) were obtained from the following proteins: aldolase, 158 kDa; cobalbumin, 75 kDa; ovalbumin, 44 kDa; and carbonic anhydrase, 29 kDa. FIG |
| 66 74 SDS-PAGE experimental_method The elution fractions, indicated by the gray shading, were run on SDS-PAGE and are shown below the gel-filtration elution profile. FIG |
| 99 129 gel-filtration elution profile evidence The elution fractions, indicated by the gray shading, were run on SDS-PAGE and are shown below the gel-filtration elution profile. FIG |
| 71 74 SEC experimental_method The schematic diagrams representing the protein constructs used in the SEC are shown on the left of each SDS-PAGE profile. FIG |
| 105 113 SDS-PAGE experimental_method The schematic diagrams representing the protein constructs used in the SEC are shown on the left of each SDS-PAGE profile. FIG |
| 20 32 Dimerization oligomeric_state Domain Swapping for Dimerization of SEL1Lcent. FIG |
| 36 45 SEL1Lcent structure_element Domain Swapping for Dimerization of SEL1Lcent. FIG |
| 4 22 Sequence alignment experimental_method (A) Sequence alignment of the SLR motifs in SEL1L. FIG |
| 30 33 SLR structure_element (A) Sequence alignment of the SLR motifs in SEL1L. FIG |
| 44 49 SEL1L protein (A) Sequence alignment of the SLR motifs in SEL1L. FIG |
| 7 10 SLR structure_element The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent. FIG |
| 23 30 aligned experimental_method The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent. FIG |
| 52 69 crystal structure evidence The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent. FIG |
| 73 82 SEL1Lcent structure_element The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent. FIG |
| 17 26 SEL1Lcent structure_element The sequences of SEL1Lcent included in the crystal structure are highlighted by the blue box. FIG |
| 43 60 crystal structure evidence The sequences of SEL1Lcent included in the crystal structure are highlighted by the blue box. FIG |
| 73 80 helices structure_element The secondary structure elements are indicated above the sequences, with helices depicted as cylinders. FIG |
| 4 6 GG structure_element The GG sequence in SLR motif 9, which creates the hinge for domain swapping (see text), is shaded yellow. FIG |
| 19 30 SLR motif 9 structure_element The GG sequence in SLR motif 9, which creates the hinge for domain swapping (see text), is shaded yellow. FIG |
| 50 55 hinge structure_element The GG sequence in SLR motif 9, which creates the hinge for domain swapping (see text), is shaded yellow. FIG |
| 81 85 SLRs structure_element Stars below the sequences indicate the specific residues that commonly appear in SLRs. FIG |
| 4 23 Structure alignment experimental_method (B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9. FIG |
| 32 35 SLR structure_element (B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9. FIG |
| 46 55 SEL1Lcent structure_element (B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9. FIG |
| 102 113 SLR motif 9 structure_element (B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9. FIG |
| 5 8 SLR structure_element Each SLR motif is shown in a different color. FIG |
| 3 14 SLR motif 9 structure_element In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 37 44 helices structure_element In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 82 85 SLR structure_element In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 102 111 α-hairpin structure_element In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 154 161 Gly 512 residue_name_number In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 166 173 Gly 513 residue_name_number In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 227 235 helix 9B structure_element In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 257 262 dimer oligomeric_state In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer. FIG |
| 4 11 Gly 512 residue_name_number The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 16 23 Gly 513 residue_name_number The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 92 107 point mutations experimental_method The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 150 157 Gly 512 residue_name_number The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 162 169 Gly 513 residue_name_number The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 206 211 hinge structure_element The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 215 226 SLR motif 9 structure_element The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 228 233 G512A mutant The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 235 240 G513A mutant The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 242 247 G512A mutant The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 248 253 G513A mutant The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 259 264 G512K mutant The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 265 270 G513K mutant The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K. FIG |
| 0 29 Size-exclusion chromatography experimental_method Size-exclusion chromatography was conducted as described in Fig. 2B. FIG |
| 0 5 SEL1L protein SEL1L forms self-oligomer mediated by the SEL1Lcent domain in vivo. FIG |
| 12 25 self-oligomer oligomeric_state SEL1L forms self-oligomer mediated by the SEL1Lcent domain in vivo. FIG |
| 42 51 SEL1Lcent structure_element SEL1L forms self-oligomer mediated by the SEL1Lcent domain in vivo. FIG |
| 94 112 immunoprecipitated experimental_method (A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 126 130 FLAG experimental_method (A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 152 164 western blot experimental_method (A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 188 190 HA experimental_method (A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 4 15 full-length protein_state The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA. FIG |
| 16 21 SEL1L protein The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA. FIG |
| 22 26 FLAG experimental_method The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA. FIG |
| 31 52 co-immunoprecipitated experimental_method The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA. FIG |
| 62 73 full-length protein_state The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA. FIG |
| 74 79 SEL1L protein The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA. FIG |
| 80 82 HA experimental_method The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA. FIG |
| 6 15 SEL1Lcent structure_element Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 20 41 co-immunoprecipitated experimental_method Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 51 62 full-length protein_state Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 63 68 SEL1L protein Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 79 90 SLR motif 9 structure_element Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 91 99 deletion experimental_method Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 249 261 western blot experimental_method Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 275 294 immunoprecipitation experimental_method Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively. FIG |
| 4 16 SEL1L348–497 mutant The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER. FIG |
| 68 77 SEL1Lcent structure_element The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER. FIG |
| 106 125 SEL1Lcent-FLAG-KDEL mutant The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER. FIG |
| 130 152 SEL1L348–497-FLAG-KDEL mutant The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER. FIG |
| 4 9 SEL1L protein The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody. FIG |
| 135 153 immunoprecipitated experimental_method The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody. FIG |
| 167 169 HA experimental_method The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody. FIG |
| 191 203 Western blot experimental_method The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody. FIG |
| 227 231 FLAG experimental_method The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody. FIG |
| 4 15 full-length protein_state The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 16 21 SEL1L protein The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 28 42 self-oligomers oligomeric_state The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 51 70 SEL1Lcent-FLAG-KDEL mutant The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 75 96 co-immunoprecipitated experimental_method The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 102 113 full-length protein_state The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 114 119 SEL1L protein The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 120 122 HA experimental_method The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA. FIG |
| 51 73 SEL1L348–497-FLAG-KDEL mutant The red asterisk indicates the expected signal for SEL1L348–497-FLAG-KDEL. FIG |
| 0 22 SEL1L348–497-FLAG-KDEL mutant SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA. FIG |
| 57 68 full-length protein_state SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA. FIG |
| 69 74 SEL1L protein SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA. FIG |
| 75 77 HA experimental_method SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA. FIG |
| 53 70 SEL1Lcent-HA-KDEL mutant The white asterisks indicate non-specific bands. (E) SEL1Lcent-HA-KDEL competitively inhibited self-oligomerization of full-length SEL1L. FIG |
| 119 130 full-length protein_state The white asterisks indicate non-specific bands. (E) SEL1Lcent-HA-KDEL competitively inhibited self-oligomerization of full-length SEL1L. FIG |
| 131 136 SEL1L protein The white asterisks indicate non-specific bands. (E) SEL1Lcent-HA-KDEL competitively inhibited self-oligomerization of full-length SEL1L. FIG |
| 54 79 immunoprecipitation assay experimental_method The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 108 112 FLAG experimental_method The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 134 146 western blot experimental_method The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 170 172 HA experimental_method The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody. FIG |
| 52 57 SEL1L protein The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L. FIG |
| 63 71 oligomer oligomeric_state The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L. FIG |
| 109 126 SEL1Lcent-HA-KDEL mutant The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L. FIG |
| 132 137 L521A mutant The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L. FIG |
| 138 150 point mutant protein_state The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L. FIG |
| 154 163 SEL1Lcent structure_element The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L. FIG |
| 204 209 SEL1L protein The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L. FIG |
| 14 17 SLR structure_element Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins. FIG |
| 21 26 SEL1L protein Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins. FIG |
| 32 35 TPR structure_element Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins. FIG |
| 45 68 SLR-Containing Proteins protein_type Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins. FIG |
| 27 42 superimposition experimental_method (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 58 61 TPR structure_element (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 73 78 Cdc23 protein (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 86 89 SLR structure_element (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 101 110 SEL1Lcent structure_element (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 123 126 SLR structure_element (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 137 141 HcpC protein (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 146 155 SEL1Lcent structure_element (A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right). FIG |
| 4 9 SEL1L protein The SEL1L, Cdc23, and HcpC are colored magenta, green and cyan, respectively. FIG |
| 11 16 Cdc23 protein The SEL1L, Cdc23, and HcpC are colored magenta, green and cyan, respectively. FIG |
| 22 26 HcpC protein The SEL1L, Cdc23, and HcpC are colored magenta, green and cyan, respectively. FIG |
| 24 39 disulfide bonds ptm The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 47 51 HcpC protein The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 57 60 Cys residue_name The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 82 99 disulfide bonding ptm The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 162 177 superimposition experimental_method The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 181 186 Cdc23 protein The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 191 200 SEL1Lcent structure_element The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 211 215 HcpC protein The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 220 229 SEL1Lcent structure_element The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 281 298 α-solenoid domain structure_element The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain. FIG |
| 5 14 SEL1Lcent structure_element Both SEL1Lcent schematics are identically oriented for comparison. FIG |
| 37 54 α-solenoid domain structure_element The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right). FIG |
| 59 71 superimposed experimental_method The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right). FIG |
| 79 106 root-mean-squared deviation evidence The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right). FIG |
| 120 125 Cdc23 protein The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right). FIG |
| 130 139 SEL1Lcent structure_element The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right). FIG |
| 162 166 HcpC protein The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right). FIG |
| 171 180 SEL1Lcent structure_element The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right). FIG |
| 0 9 SEL1Lcent structure_element SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping. FIG |
| 11 16 Cdc23 protein SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping. FIG |
| 22 26 HcpC protein SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping. FIG |
| 89 98 structure evidence SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping. FIG |
| 102 107 Cdc23 protein SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping. FIG |
| 125 134 SEL1Lcent structure_element SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping. FIG |
| 183 188 dimer oligomeric_state SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping. FIG |
| 12 17 SLR-C structure_element The Role of SLR-C in ERAD machinery and Model for the Organization of Proteins in Membrane-Associated ERAD Components. FIG |
| 34 38 HRD1 protein (A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L. FIG |
| 71 84 GST pull-down experimental_method (A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L. FIG |
| 101 122 Pull-down experiments experimental_method (A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L. FIG |
| 159 162 HRD complex_assembly (A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L. FIG |
| 163 176 luminal loops structure_element (A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L. FIG |
| 189 192 SLR structure_element (A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L. FIG |
| 203 208 SEL1L protein (A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L. FIG |
| 17 29 luminal loop structure_element Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 33 37 HRD1 protein Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 47 50 GST chemical Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 145 148 SLR structure_element Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 160 167 monomer oligomeric_state Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 176 181 SLR-M structure_element Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 183 193 SLR-ML521A mutant Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 211 216 SEL1L protein Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L. FIG |
| 30 38 SDS-PAGE experimental_method Proteins were analyzed by 12% SDS-PAGE and Coomassie blue staining. FIG |
| 52 60 metazoan taxonomy_domain (C) Schematic representation of the organization of metazoan ERAD components in the ER membrane. FIG |
| 7 10 SLR structure_element The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein. FIG |
| 21 26 SEL1L protein The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein. FIG |
| 91 96 SLR-N structure_element The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein. FIG |
| 98 103 SLR-M structure_element The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein. FIG |
| 109 114 SLR-C structure_element The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein. FIG |
| 129 147 sequence alignment experimental_method The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein. FIG |
| 174 191 crystal structure evidence The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein. FIG |
| 37 40 SLR structure_element We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen. FIG |
| 51 56 SEL1L protein We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen. FIG |
| 95 100 SLR-M structure_element We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen. FIG |
| 118 123 dimer oligomeric_state We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen. FIG |
| 154 159 SLR-C structure_element We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen. FIG |
| 196 200 HRD1 protein We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen. FIG |
| 30 39 SEL1Lcent structure_element The surface representation of SEL1Lcent is placed in the same orientation as that shown in the schematic model to show that the putative N-glycosylation site, residue N427 (indicated in yellow), is exposed on the surface of the protein. FIG |
| 137 157 N-glycosylation site site The surface representation of SEL1Lcent is placed in the same orientation as that shown in the schematic model to show that the putative N-glycosylation site, residue N427 (indicated in yellow), is exposed on the surface of the protein. FIG |
| 167 171 N427 residue_name_number The surface representation of SEL1Lcent is placed in the same orientation as that shown in the schematic model to show that the putative N-glycosylation site, residue N427 (indicated in yellow), is exposed on the surface of the protein. FIG |
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