6OO7

Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in nanodiscs

6OO7 の概要

• エントリーDOI: 10.2210/pdb6oo7/pdb
• EMDBエントリー: 20143 20145 20146 20148
• 分子名称: TRPV2, resiniferatoxin (2 entities in total)
• 機能のキーワード: ion channel, calcium channel, trp channel, metal transport
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 357405.55

構造登録者

Zubcevic, L.,Hsu, A.L.,Borgnia, M.J.,Lee, S.-Y. (登録日: 2019-04-22, 公開日: 2019-05-29, 最終更新日: 2024-03-20)

主引用文献

Zubcevic, L.,Hsu, A.L.,Borgnia, M.J.,Lee, S.Y.
Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes.
Elife, 8:-, 2019

PubMed Abstract: The Transient Receptor Potential Vanilloid 2 (TRPV2) channel is a member of the temperature-sensing thermoTRPV family. Recent advances in cryo-electronmicroscopy (cryo-EM) and X-ray crystallography have provided many important insights into the gating mechanisms of thermoTRPV channels. Interestingly, crystallographic studies of ligand-dependent TRPV2 gating have shown that the TRPV2 channel adopts two-fold symmetric arrangements during the gating cycle. However, it was unclear if crystal packing forces played a role in stabilizing the two-fold symmetric arrangement of the channel. Here, we employ cryo-EM to elucidate the structure of full-length rabbit TRPV2 in complex with the agonist resiniferatoxin (RTx) in nanodiscs and amphipol. We show that RTx induces two-fold symmetric conformations of TRPV2 in both environments. However, the two-fold symmetry is more pronounced in the native-like lipid environment of the nanodiscs. Our data offers insights into a gating pathway in TRPV2 involving symmetry transitions.

PubMed: 31090543
DOI: 10.7554/eLife.45779

実験手法

ELECTRON MICROSCOPY (3.8 Å)