6OT5

Structure of the TRPV3 K169A sensitized mutant in the presence of 2-APB at 3.6 A resolution

6OT5 の概要

• エントリーDOI: 10.2210/pdb6ot5/pdb
• EMDBエントリー: 20192 20194
• 分子名称: Transient receptor potential cation channel subfamily V member 3,Transient receptor potential cation channel subfamily V member 3, 2-aminoethyl diphenylborinate (2 entities in total)
• 機能のキーワード: ion channel, trp channel, trpv channel, metal transport, membrane transport, membrane protein, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 332827.81

構造登録者

Zubcevic, L.,Borschel, W.F.,Hsu, A.L.,Borgnia, M.J.,Lee, S.-Y. (登録日: 2019-05-02, 公開日: 2019-05-22, 最終更新日: 2025-05-28)

主引用文献

Zubcevic, L.,Borschel, W.F.,Hsu, A.L.,Borgnia, M.J.,Lee, S.Y.
Regulatory switch at the cytoplasmic interface controls TRPV channel gating.
Elife, 8:-, 2019

PubMed Abstract: Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a β-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here, we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes.

PubMed: 31070581
DOI: 10.7554/eLife.47746

実験手法

ELECTRON MICROSCOPY (3.6 Å)