5ZBG

Cryo-EM structure of human TRPC3 at 4.36A resolution

5ZBG の概要

• エントリーDOI: 10.2210/pdb5zbg/pdb
• EMDBエントリー: 6911
• 分子名称: Short transient receptor potential channel 3 (1 entity in total)
• 機能のキーワード: trpc3 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: 389863.34

構造登録者

Chen, L.,Tang, Q.,Guo, W. (登録日: 2018-02-11, 公開日: 2018-05-09, 最終更新日: 2024-03-27)

主引用文献

Tang, Q.,Guo, W.,Zheng, L.,Wu, J.X.,Liu, M.,Zhou, X.,Zhang, X.,Chen, L.
Structure of the receptor-activated human TRPC6 and TRPC3 ion channels
Cell Res., 28:746-755, 2018

PubMed Abstract: TRPC6 and TRPC3 are receptor-activated nonselective cation channels that belong to the family of canonical transient receptor potential (TRPC) channels. They are activated by diacylglycerol, a lipid second messenger. TRPC6 and TRPC3 are involved in many physiological processes and implicated in human genetic diseases. Here we present the structure of human TRPC6 homotetramer in complex with a newly identified high-affinity inhibitor BTDM solved by single-particle cryo-electron microscopy to 3.8 Å resolution. We also present the structure of human TRPC3 at 4.4 Å resolution. These structures show two-layer architectures in which the bell-shaped cytosolic layer holds the transmembrane layer. Extensive inter-subunit interactions of cytosolic domains, including the N-terminal ankyrin repeats and the C-terminal coiled-coil, contribute to the tetramer assembly. The high-affinity inhibitor BTDM wedges between the S5-S6 pore domain and voltage sensor-like domain to inhibit channel opening. Our structures uncover the molecular architecture of TRPC channels and provide a structural basis for understanding the mechanism of these channels.

PubMed: 29700422
DOI: 10.1038/s41422-018-0038-2

実験手法

ELECTRON MICROSCOPY (4.36 Å)