3J5Q

Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy

3J5Q の概要

• エントリーDOI: 10.2210/pdb3j5q/pdb
• 関連するPDBエントリー: 3J5P 3J5R
• EMDBエントリー: 5776 5777 5778
• 分子名称: Transient receptor potential cation channel subfamily V member 1, Kappa-theraphotoxin-Cg1a 1 (2 entities in total)
• 機能のキーワード: trpv1 channel, dktx, rtx, transport protein-toxin complex, transport protein/toxin
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 296912.90

構造登録者

Liao, M.,Cao, E.,Julius, D.,Cheng, Y. (登録日: 2013-10-28, 公開日: 2013-12-04, 最終更新日: 2024-05-15)

主引用文献

Cao, E.,Liao, M.,Cheng, Y.,Julius, D.
TRPV1 structures in distinct conformations reveal activation mechanisms.
Nature, 504:113-118, 2013

PubMed Abstract: Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide range of physical and chemical stimuli. Elucidating how these channels integrate and convert physiological signals into channel opening is essential to understanding how they regulate cell excitability under normal and pathophysiological conditions. Here we exploit pharmacological probes (a peptide toxin and small vanilloid agonists) to determine structures of two activated states of the capsaicin receptor, TRPV1. A domain (consisting of transmembrane segments 1-4) that moves during activation of voltage-gated channels remains stationary in TRPV1, highlighting differences in gating mechanisms for these structurally related channel superfamilies. TRPV1 opening is associated with major structural rearrangements in the outer pore, including the pore helix and selectivity filter, as well as pronounced dilation of a hydrophobic constriction at the lower gate, suggesting a dual gating mechanism. Allosteric coupling between upper and lower gates may account for rich physiological modulation exhibited by TRPV1 and other TRP channels.

PubMed: 24305161
DOI: 10.1038/nature12823

実験手法

ELECTRON MICROSCOPY (3.8 Å)