5B26

Crystal structure of mouse SEL1L

5B26 の概要

• エントリーDOI: 10.2210/pdb5b26/pdb
• 分子名称: Protein sel-1 homolog 1 (2 entities in total)
• 機能のキーワード: sel1l, slr motif, erad, signaling protein
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Endoplasmic reticulum membrane ; Single-pass type I membrane protein : Q9Z2G6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 82043.96

構造登録者

Jeong, H.,Lee, C. (登録日: 2016-01-09, 公開日: 2016-04-27, 最終更新日: 2024-03-20)

主引用文献

Jeong, H.,Sim, H.J.,Song, E.K.,Lee, H.,Ha, S.C.,Jun, Y.,Park, T.J.,Lee, C.
Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway
Sci Rep, 6:20261-20261, 2016

PubMed Abstract: 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.

PubMed: 27064360
DOI: 10.1038/srep20261

実験手法

X-RAY DIFFRACTION (2.6 Å)