5GJV

Structure of the mammalian voltage-gated calcium channel Cav1.1 complex at near atomic resolution

5GJV の概要

• エントリーDOI: 10.2210/pdb5gjv/pdb
• EMDBエントリー: 9513
• 関連するBIRD辞書のPRD_ID: PRD_900017
• 分子名称: Voltage-dependent L-type calcium channel subunit alpha-1S, 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE, CALCIUM ION, ... (11 entities in total)
• 機能のキーワード: complex, channel, membrane protein
• 由来する生物種: Oryctolagus cuniculus (Rabbit); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 413260.63

構造登録者

Wu, J.P.,Yan, Z.,Li, Z.Q.,Zhou, Q.,Yan, N. (登録日: 2016-07-02, 公開日: 2016-09-14, 最終更新日: 2024-11-20)

主引用文献

Wu, J.P.,Yan, Z.,Li, Z.Q.,Qian, X.Y.,Lu, S.,Dong, M.Q.,Zhou, Q.,Yan, N.
Structure of the voltage-gated calcium channel Cav1.1 at 3.6 angstrom resolution
Nature, 537:191-196, 2016

PubMed Abstract: The voltage-gated calcium (Ca) channels convert membrane electrical signals to intracellular Ca-mediated events. Among the ten subtypes of Ca channel in mammals, Ca1.1 is specified for the excitation-contraction coupling of skeletal muscles. Here we present the cryo-electron microscopy structure of the rabbit Ca1.1 complex at a nominal resolution of 3.6 Å. The inner gate of the ion-conducting α1-subunit is closed and all four voltage-sensing domains adopt an 'up' conformation, suggesting a potentially inactivated state. The extended extracellular loops of the pore domain, which are stabilized by multiple disulfide bonds, form a windowed dome above the selectivity filter. One side of the dome provides the docking site for the α2δ-1-subunit, while the other side may attract cations through its negative surface potential. The intracellular I-II and III-IV linker helices interact with the β-subunit and the carboxy-terminal domain of α1, respectively. Classification of the particles yielded two additional reconstructions that reveal pronounced displacement of β and adjacent elements in α1. The atomic model of the Ca1.1 complex establishes a foundation for mechanistic understanding of excitation-contraction coupling and provides a three-dimensional template for molecular interpretations of the functions and disease mechanisms of Ca and Na channels.

PubMed: 27580036
DOI: 10.1038/nature19321

実験手法

ELECTRON MICROSCOPY (3.6 Å)