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3J8H

Structure of the rabbit ryanodine receptor RyR1 in complex with FKBP12 at 3.8 Angstrom resolution

これはPDB形式変換不可エントリーです。
3J8H の概要
エントリーDOI10.2210/pdb3j8h/pdb
EMDBエントリー2807
分子名称Ryanodine receptor 1, Peptidyl-prolyl cis-trans isomerase FKBP1A, ZINC ION (3 entities in total)
機能のキーワードrabbit ryanodine receptor ryr1, high-conductance intracellular ca2+ channels, excitation-contraction coupling, transport protein-isomerase complex, transport protein/isomerase
由来する生物種Oryctolagus cuniculus (rabbit)
詳細
タンパク質・核酸の鎖数8
化学式量合計2048453.92
構造登録者
Yan, Z.,Bai, X.,Yan, C.,Wu, J.,Scheres, S.H.W.,Shi, Y.,Yan, N. (登録日: 2014-10-26, 公開日: 2014-12-10, 最終更新日: 2024-02-21)
主引用文献Yan, Z.,Bai, X.C.,Yan, C.,Wu, J.,Li, Z.,Xie, T.,Peng, W.,Yin, C.C.,Li, X.,Scheres, S.H.,Shi, Y.,Yan, N.
Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution.
Nature, 517:50-55, 2015
Cited by
PubMed Abstract: The ryanodine receptors (RyRs) are high-conductance intracellular Ca(2+) channels that play a pivotal role in the excitation-contraction coupling of skeletal and cardiac muscles. RyRs are the largest known ion channels, with a homotetrameric organization and approximately 5,000 residues in each protomer. Here we report the structure of the rabbit RyR1 in complex with its modulator FKBP12 at an overall resolution of 3.8 Å, determined by single-particle electron cryomicroscopy. Three previously uncharacterized domains, named central, handle and helical domains, display the armadillo repeat fold. These domains, together with the amino-terminal domain, constitute a network of superhelical scaffold for binding and propagation of conformational changes. The channel domain exhibits the voltage-gated ion channel superfamily fold with distinct features. A negative-charge-enriched hairpin loop connecting S5 and the pore helix is positioned above the entrance to the selectivity-filter vestibule. The four elongated S6 segments form a right-handed helical bundle that closes the pore at the cytoplasmic border of the membrane. Allosteric regulation of the pore by the cytoplasmic domains is mediated through extensive interactions between the central domains and the channel domain. These structural features explain high ion conductance by RyRs and the long-range allosteric regulation of channel activities.
PubMed: 25517095
DOI: 10.1038/nature14063
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.8 Å)
構造検証レポート
Validation report summary of 3j8h
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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