6BQR

Human TRPM4 ion channel in lipid nanodiscs in a calcium-free state

6BQR の概要

• エントリーDOI: 10.2210/pdb6bqr/pdb
• EMDBエントリー: 7132 7133
• 分子名称: Transient receptor potential cation channel subfamily M member 4, CHOLESTEROL HEMISUCCINATE (2 entities in total)
• 機能のキーワード: trpm4, trpm channel, trp channel, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 491752.52

構造登録者

Autzen, H.E.,Myasnikov, A.G.,Campbell, M.G.,Asarnow, D.,Julius, D.,Cheng, Y. (登録日: 2017-11-28, 公開日: 2017-12-20, 最終更新日: 2019-12-18)

主引用文献

Autzen, H.E.,Myasnikov, A.G.,Campbell, M.G.,Asarnow, D.,Julius, D.,Cheng, Y.
Structure of the human TRPM4 ion channel in a lipid nanodisc.
Science, 359:228-232, 2018

PubMed Abstract: Transient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular calcium in a voltage-dependent manner but, unlike many other TRP channels, is permeable to monovalent cations only. Here we present two structures of full-length human TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo-electron microscopy. These structures, with and without calcium bound, reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain. The structures correspond to two distinct closed states. Calcium binding induces conformational changes that likely prime the channel for voltage-dependent opening.

PubMed: 29217581
DOI: 10.1126/science.aar4510

実験手法

ELECTRON MICROSCOPY (3.2 Å)