5b26 | pdb_00005b26
Crystal structure of mouse SEL1L
Structural highlights
Function[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). Publication Abstract from PubMedTerminally 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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