2K60

NMR structure of calcium-loaded STIM1 EF-SAM

2K60 の概要

• エントリーDOI: 10.2210/pdb2k60/pdb
• NMR情報: BMRB: 15851
• 分子名称: PROTEIN (Stromal interaction molecule 1), CALCIUM ION (2 entities in total)
• 機能のキーワード: ef-hand, sam domain, ef-sam, stim1, stromal interaction molecule, store operated calcium entry regulator, soce, endoplasmic reticulum luminal calcium sensor, calcium transport, glycoprotein, ion transport, membrane, phosphoprotein, transmembrane, transport, transport protein, signaling protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: Q13586
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17420.45

構造登録者

Stathopulos, P.B.,Ikura, M. (登録日: 2008-07-02, 公開日: 2008-10-07, 最終更新日: 2024-05-01)

主引用文献

Stathopulos, P.B.,Zheng, L.,Li, G.Y.,Plevin, M.J.,Ikura, M.
Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry.
Cell(Cambridge,Mass.), 135:110-122, 2008

PubMed Abstract: Stromal interaction molecule-1 (STIM1) activates store-operated Ca2+ entry (SOCE) in response to diminished luminal Ca2+ levels. Here, we present the atomic structure of the Ca2+-sensing region of STIM1 consisting of the EF-hand and sterile alpha motif (SAM) domains (EF-SAM). The canonical EF-hand is paired with a previously unidentified EF-hand. Together, the EF-hand pair mediates mutually indispensable hydrophobic interactions between the EF-hand and SAM domains. Structurally critical mutations in the canonical EF-hand, "hidden" EF-hand, or SAM domain disrupt Ca2+ sensitivity in oligomerization via destabilization of the entire EF-SAM entity. In mammalian cells, EF-SAM destabilization mutations within full-length STIM1 induce punctae formation and activate SOCE independent of luminal Ca2+. We provide atomic resolution insight into the molecular basis for STIM1-mediated SOCE initiation and show that the folded/unfolded state of the Ca2+-sensing region of STIM is crucial to SOCE regulation.

PubMed: 18854159
DOI: 10.1016/j.cell.2008.08.006

実験手法

SOLUTION NMR