3TER

Crystal structure of SOAR domain with Inhibition helix from C. elegans

3TER の概要

• エントリーDOI: 10.2210/pdb3ter/pdb
• 分子名称: Mammalian stromal interaction molecule-1 (2 entities in total)
• 機能のキーワード: dimer, metal binding protein
• 由来する生物種: Caenorhabditis elegans (nematode)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31233.69

構造登録者

Yang, X.,Jin, H.,Cai, X.,Shen, Y. (登録日: 2011-08-15, 公開日: 2012-04-11, 最終更新日: 2024-03-20)

主引用文献

Yang, X.,Jin, H.,Cai, X.,Li, S.,Shen, Y.
Structural and mechanistic insights into the activation of Stromal interaction molecule 1 (STIM1).
Proc.Natl.Acad.Sci.USA, 109:5657-5662, 2012

PubMed Abstract: Calcium influx through the Ca(2+) release-activated Ca(2+) (CRAC) channel is an essential process in many types of cells. Upon store depletion, the calcium sensor in the endoplasmic reticulum, STIM1, activates Orai1, a CRAC channel in the plasma membrane. We have determined the structures of SOAR from Homo sapiens (hSOAR), which is part of STIM1 and is capable of constitutively activating Orai1, and the entire coiled coil region of STIM1 from Caenorhabditis elegans (ceSTIM1-CCR) in an inactive state. Our studies reveal that the formation of a SOAR dimer is necessary to activate the Orai1 channel. Mutations that disrupt SOAR dimerization or remove the cluster of positive residues abolish STIM1 activation of Orai1. We identified a possible inhibitory helix within the structure of ceSTIM1-CCR that tightly interacts with SOAR. Functional studies suggest that the inhibitory helix may keep the C-terminus of STIM1 in an inactive state. Our data allowed us to propose a model for STIM1 activation.

PubMed: 22451904
DOI: 10.1073/pnas.1118947109

実験手法

X-RAY DIFFRACTION (2.551 Å)