9KDB

Structure of hTRPC3 in complex with Nb1-25 at 2.67 angstrom

これはPDB形式変換不可エントリーです。

9KDB の概要

• エントリーDOI: 10.2210/pdb9kdb/pdb
• EMDBエントリー: 62268
• 分子名称: Nb1-25, Short transient receptor potential channel 3, ZINC ION, ... (5 entities in total)
• 機能のキーワード: trpc3, dag, nb1-25, nanobody, metal transport
• 由来する生物種: Camelus; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 507556.76

構造登録者

Chen, L.,Guo, W.,Chen, Y.,Zang, J. (登録日: 2024-11-03, 公開日: 2025-10-08, 最終更新日: 2025-11-12)

主引用文献

Chen, Y.,Zang, J.,Guo, W.,Xu, J.,Wei, M.,Quan, L.,Zhu, M.,Zhao, X.,Peng, H.,Wan, Y.,Chen, L.
Structural mechanism of the agonist binding on human TRPC3 channel.
Nat Commun, 16:9343-9343, 2025

PubMed Abstract: TRPC3/6/7 channels are cation channels that are directly activated by the second messenger diacylglycerol (DAG). These channels play crucial physiological roles and are implicated in various disease conditions; however, the binding mechanism of DAG to these channels remains incompletely understood. In this study, we present the structures of human TRPC3 in complex with DAG or synthetic activators, 4n and GSK1702934A. The structural analysis reveals that DAG binds at the L2 site, located near the pore on the extracellular side of TRPC3. Functional assays confirmed that the L2 site serves as the activating site for DAG. Notably, both 4n and GSK1702934A competitively bind to the same site, facilitating channel activation. Moreover, based on the pharmacophore identified from the DAG-bound structure, we found that monoacylglycerols (MAGs) are endogenous activators of TRPC3/6/7 channels, providing new insights into their regulatory mechanisms.

PubMed: 41125595
DOI: 10.1038/s41467-025-64435-6

実験手法

ELECTRON MICROSCOPY (2.67 Å)