6KG7

Cryo-EM Structure of the Mammalian Tactile Channel Piezo2

6KG7 の概要

• エントリーDOI: 10.2210/pdb6kg7/pdb
• EMDBエントリー: 9975
• 分子名称: Piezo-type mechanosensitive ion channel component 2, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: piezo, mechanogating, mechanotransduction channel, membrane protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 980609.03

構造登録者

Wang, L.,Zhou, H.,Zhang, M.,Liu, W.,Deng, T.,Zhao, Q.,Li, Y.,Lei, J.,Li, X.,Xiao, B. (登録日: 2019-07-11, 公開日: 2019-09-04, 最終更新日: 2024-10-09)

主引用文献

Wang, L.,Zhou, H.,Zhang, M.,Liu, W.,Deng, T.,Zhao, Q.,Li, Y.,Lei, J.,Li, X.,Xiao, B.
Structure and mechanogating of the mammalian tactile channel PIEZO2.
Nature, 573:225-229, 2019

PubMed Abstract: PIEZO2 is a mechanosensitive cation channel that has a key role in sensing touch, tactile pain, breathing and blood pressure. Here we describe the cryo-electron microscopy structure of mouse PIEZO2, which is a three-bladed, propeller-like trimer that comprises 114 transmembrane helices (38 per protomer). Transmembrane helices 1-36 (TM1-36) are folded into nine tandem units of four transmembrane helices each to form the unusual non-planar blades. The three blades are collectively curved into a nano-dome of 28-nm diameter and 10-nm depth, with an extracellular cap-like structure embedded in the centre and a 9-nm-long intracellular beam connecting to the central pore. TM38 and the C-terminal domain are surrounded by the anchor domain and TM37, and enclose the central pore with both transmembrane and cytoplasmic constriction sites. Structural comparison between PIEZO2 and its homologue PIEZO1 reveals that the transmembrane constriction site might act as a transmembrane gate that is controlled by the cap domain. Together, our studies provide insights into the structure and mechanogating mechanism of Piezo channels.

PubMed: 31435011
DOI: 10.1038/s41586-019-1505-8

実験手法

ELECTRON MICROSCOPY (3.8 Å)