5b26

</td></tr><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>

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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