8YMX

The structure of BRTNaC1 at 40 degree centigrade

8YMX の概要

• エントリーDOI: 10.2210/pdb8ymx/pdb
• EMDBエントリー: 39410
• 分子名称: Broad-range thermal receptor 1 (1 entity in total)
• 機能のキーワード: brtnac1, membrane protein, trimer
• 由来する生物種: Scolopendra mutilans
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 147931.02

構造登録者

Yuan, L.,Chen, X.,Su, N. (登録日: 2024-03-10, 公開日: 2025-03-05, 最終更新日: 2025-07-23)

主引用文献

Chen, X.,Yuan, L.,Wen, H.,Ma, Q.,Deng, Z.,Xu, Y.,Yao, Z.,Wang, Y.,Yang, S.,Su, N.,Yang, F.
Structure and function of a broad-range thermal receptor in myriapods.
Nat.Struct.Mol.Biol., 32:1081-1090, 2025

PubMed Abstract: Broad-range thermal receptor 1 (BRTNaC1), activated by heat at low extracellular pH, was recently identified in myriapods. Although the overexpression of BRTNaC1 leads to robust heat-activated current with a cation selectivity profile, the structure of this receptor and how it is gated by proton and heat remain to be investigated. Here we determine cryogenic electron microscopy structures of BRTNaC1 in the apo, proton-induced and heated states. Based on these structures, patch-clamp recordings and molecular dynamic simulations, we found that a 'twist the wrist' mechanism is used for proton activation of BRTNaC1, while heat induces broad conformational changes in BRTNaC1, including rotation and shift in the transmembrane helices to open this channel. Moreover, as testosterone inhibited BRTNaC1 activation, we identified four clustered residues important for such inhibition. Therefore, our study has established the structural basis for ligand and temperature gating in the BRTNaC1 ion channel.

PubMed: 40011748
DOI: 10.1038/s41594-025-01495-8

実験手法

ELECTRON MICROSCOPY (3.27 Å)