2L5Y

NMR structure of calcium-loaded STIM2 EF-SAM.

2L5Y の概要

• エントリーDOI: 10.2210/pdb2l5y/pdb
• NMR情報: BMRB: 17289
• 分子名称: Stromal interaction molecule 2, CALCIUM ION (2 entities in total)
• 機能のキーワード: stromal interaction molecule, ef-hand, sam domain, store operated calcium entry, signaling protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17871.05

構造登録者

Zheng, L.,Stathopulos, P.B.,Ikura, M. (登録日: 2010-11-09, 公開日: 2011-01-19, 最終更新日: 2024-05-01)

主引用文献

Zheng, L.,Stathopulos, P.B.,Schindl, R.,Li, G.Y.,Romanin, C.,Ikura, M.
Auto-inhibitory role of the EF-SAM domain of STIM proteins in store-operated calcium entry.
Proc.Natl.Acad.Sci.USA, 108:1337-1342, 2011

PubMed Abstract: Stromal interaction molecules (STIM)s function as endoplasmic reticulum calcium (Ca(2+)) sensors that differentially regulate plasma membrane Ca(2+) release activated Ca(2+) channels in various cells. To probe the structural basis for the functional differences between STIM1 and STIM2 we engineered a series of EF-hand and sterile α motif (SAM) domain (EF-SAM) chimeras, demonstrating that the STIM1 Ca(2+)-binding EF-hand and the STIM2 SAM domain are major contributors to the autoinhibition of oligomerization in each respective isoform. Our nuclear magnetic resonance (NMR) derived STIM2 EF-SAM structure provides a rationale for an augmented stability, which involves a 54° pivot in the EF-hand:SAM domain orientation permissible by an expanded nonpolar cleft, ionic interactions, and an enhanced hydrophobic SAM core, unique to STIM2. Live cells expressing "super-unstable" or "super-stable" STIM1/STIM2 EF-SAM chimeras in the full-length context show a remarkable correlation with the in vitro data. Together, our data suggest that divergent Ca(2+)- and SAM-dependent stabilization of the EF-SAM fold contributes to the disparate regulation of store-operated Ca(2+) entry by STIM1 and STIM2.

PubMed: 21217057
DOI: 10.1073/pnas.1015125108

実験手法

SOLUTION NMR