6G1K

Electron cryo-microscopy structure of the canonical TRPC4 ion channel

6G1K の概要

• エントリーDOI: 10.2210/pdb6g1k/pdb
• EMDBエントリー: 4339
• 分子名称: Transient receptor potential cation channel subfamily c member 4a, CHOLESTEROL HEMISUCCINATE, (2R)-3-(phosphonooxy)propane-1,2-diyl dihexanoate (3 entities in total)
• 機能のキーワード: ion channel, trpc4, ankyrin repeats, cirb domain, membrane protein, transport protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 427158.34

構造登録者

Vinayagam, D.,Mager, T.,Apelbaum, A.,Bothe, A.,Merino, F.,Hofnagel, O.,Gatsogiannis, C.,Raunser, S. (登録日: 2018-03-21, 公開日: 2018-05-02, 最終更新日: 2024-11-13)

主引用文献

Vinayagam, D.,Mager, T.,Apelbaum, A.,Bothe, A.,Merino, F.,Hofnagel, O.,Gatsogiannis, C.,Raunser, S.
Electron cryo-microscopy structure of the canonical TRPC4 ion channel.
Elife, 7:-, 2018

PubMed Abstract: Canonical transient receptor channels (TRPC) are non-selective cation channels. They are involved in receptor-operated Ca signaling and have been proposed to act as store-operated channels (SOC). Their malfunction is related to cardiomyopathies and their modulation by small molecules has been shown to be effective against renal cancer cells. The molecular mechanism underlying the complex activation and regulation is poorly understood. Here, we report the electron cryo-microscopy structure of zebrafish TRPC4 in its unliganded (apo), closed state at an overall resolution of 3.6 Å. The structure reveals the molecular architecture of the cation conducting pore, including the selectivity filter and lower gate. The cytoplasmic domain contains two key hubs that have been shown to interact with modulating proteins. Structural comparisons with other TRP channels give novel insights into the general architecture and domain organization of this superfamily of channels and help to understand their function and pharmacology.

PubMed: 29717981
DOI: 10.7554/eLife.36615

実験手法

ELECTRON MICROSCOPY (3.6 Å)