7MZC

Cryo-EM structure of minimal TRPV1 with RTX bound in C1 state

7MZC の概要

• エントリーDOI: 10.2210/pdb7mzc/pdb
• EMDBエントリー: 24083 24084 24085 24086 24087 24088 24089 24090 24091
• 分子名称: Transient receptor potential cation channel subfamily V member 1, resiniferatoxin, SODIUM ION (3 entities in total)
• 機能のキーワード: trp channel, cryo-em, nanodisc, vanilloid agonist, transport protein
• 由来する生物種: Rattus norvegicus (Rat)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 294626.22

構造登録者

Zhang, K.,Julius, D.,Cheng, Y. (登録日: 2021-05-24, 公開日: 2021-09-22, 最終更新日: 2024-10-23)

主引用文献

Zhang, K.,Julius, D.,Cheng, Y.
Structural snapshots of TRPV1 reveal mechanism of polymodal functionality.
Cell, 184:5138-, 2021

PubMed Abstract: Many transient receptor potential (TRP) channels respond to diverse stimuli and conditionally conduct small and large cations. Such functional plasticity is presumably enabled by a uniquely dynamic ion selectivity filter that is regulated by physiological agents. What is currently missing is a "photo series" of intermediate structural states that directly address this hypothesis and reveal specific mechanisms behind such dynamic channel regulation. Here, we exploit cryoelectron microscopy (cryo-EM) to visualize conformational transitions of the capsaicin receptor, TRPV1, as a model to understand how dynamic transitions of the selectivity filter in response to algogenic agents, including protons, vanilloid agonists, and peptide toxins, permit permeation by small and large organic cations. These structures also reveal mechanisms governing ligand binding substates, as well as allosteric coupling between key sites that are proximal to the selectivity filter and cytoplasmic gate. These insights suggest a general framework for understanding how TRP channels function as polymodal signal integrators.

PubMed: 34496225
DOI: 10.1016/j.cell.2021.08.012

実験手法

ELECTRON MICROSCOPY (3.03 Å)