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5b26

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==Crystal structure of mouse SEL1L==
==Crystal structure of mouse SEL1L==
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<StructureSection load='5b26' size='340' side='right' caption='[[5b26]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='5b26' size='340' side='right'caption='[[5b26]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b26]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B26 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b26]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B26 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b26 OCA], [http://pdbe.org/5b26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b26 RCSB], [http://www.ebi.ac.uk/pdbsum/5b26 PDBsum]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b26 OCA], [https://pdbe.org/5b26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b26 RCSB], [https://www.ebi.ac.uk/pdbsum/5b26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b26 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SE1L1_MOUSE SE1L1_MOUSE]] May play a role in Notch signaling. May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (By similarity).
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[https://www.uniprot.org/uniprot/SE1L1_MOUSE SE1L1_MOUSE] May play a role in Notch signaling. May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Terminally misfolded proteins are selectively recognized and cleared by the endoplasmic reticulum-associated degradation (ERAD) pathway. SEL1L, a component of the ERAD machinery, plays an important role in selecting and transporting ERAD substrates for degradation. We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1L(cent)). Strikingly, SEL1L(cent) forms a homodimer with two-fold symmetry in a head-to-tail manner. Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface. We identified that the full-length SEL1L forms a self-oligomer through the SEL1L(cent) domain in mammalian cells. 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. Therefore, we propose that certain SLR motifs of SEL1L play a unique role in membrane bound ERAD machinery.
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Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway.,Jeong H, Sim HJ, Song EK, Lee H, Ha SC, Jun Y, Park TJ, Lee C Sci Rep. 2016 Feb 9;6:20261. doi: 10.1038/srep20261. PMID:27064360<ref>PMID:27064360</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5b26" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Jeong, H]]
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[[Category: Large Structures]]
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[[Category: Lee, C]]
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[[Category: Mus musculus]]
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[[Category: Erad]]
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[[Category: Jeong H]]
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[[Category: Sel1l]]
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[[Category: Lee C]]
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[[Category: Signaling protein]]
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[[Category: Slr motif]]
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Current revision

Crystal structure of mouse SEL1L

PDB ID 5b26

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