6JRR

Structure of RyR2 (*F/A/C/L-Ca2+ dataset)

これはPDB形式変換不可エントリーです。

6JRR の概要

• エントリーDOI: 10.2210/pdb6jrr/pdb
• EMDBエントリー: 9879
• 分子名称: RyR2, Peptidyl-prolyl cis-trans isomerase FKBP1B, ZINC ION, ... (6 entities in total)
• 機能のキーワード: cryo-em, membrane protein, membrane protein-isomerase complex, membrane protein/isomerase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 2310043.94

構造登録者

Gong, D.S.,Chi, X.M.,Zhou, G.W.,Huang, G.X.Y.,Lei, J.L.,Yan, N. (登録日: 2019-04-05, 公開日: 2019-07-17, 最終更新日: 2024-03-27)

主引用文献

Gong, D.,Chi, X.,Wei, J.,Zhou, G.,Huang, G.,Zhang, L.,Wang, R.,Lei, J.,Chen, S.R.W.,Yan, N.
Modulation of cardiac ryanodine receptor 2 by calmodulin.
Nature, 572:347-351, 2019

PubMed Abstract: The high-conductance intracellular calcium (Ca) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca-dependent manner. Here we reveal the regulatory mechanism by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under eight conditions. Apo-CaM and Ca-CaM bind to distinct but overlapping sites in an elongated cleft formed by the handle, helical and central domains. The shift in CaM-binding sites on RyR2 is controlled by Ca binding to CaM, rather than to RyR2. Ca-CaM induces rotations and intradomain shifts of individual central domains, resulting in pore closure of the PCB95 and Ca-activated channel. By contrast, the pore of the ATP, caffeine and Ca-activated channel remains open in the presence of Ca-CaM, which suggests that Ca-CaM is one of the many competing modulators of RyR2 gating.

PubMed: 31278385
DOI: 10.1038/s41586-019-1377-y

実験手法

ELECTRON MICROSCOPY (3.9 Å)