6C8F

Crystal structure of Transient Receptor Potential (TRP) channel TRPV4 in the presence of cesium

6C8F の概要

• エントリーDOI: 10.2210/pdb6c8f/pdb
• 分子名称: Transient receptor potential cation channel, subfamily V, member 4, CESIUM ION (2 entities in total)
• 機能のキーワード: ion channal, transport protein
• 由来する生物種: Xenopus tropicalis (Western clawed frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 77201.58

構造登録者

Deng, Z.,Paknejad, N.,Maksaev, G.,Sala-Rabanal, M.,Nichols, C.G.,Hite, R.K.,Yuan, P. (登録日: 2018-01-24, 公開日: 2018-02-28, 最終更新日: 2023-10-04)

主引用文献

Deng, Z.,Paknejad, N.,Maksaev, G.,Sala-Rabanal, M.,Nichols, C.G.,Hite, R.K.,Yuan, P.
Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms.
Nat. Struct. Mol. Biol., 25:252-260, 2018

PubMed Abstract: The transient receptor potential (TRP) channel TRPV4 participates in multiple biological processes, and numerous TRPV4 mutations underlie several distinct and devastating diseases. Here we present the cryo-EM structure of Xenopus tropicalis TRPV4 at 3.8-Å resolution. The ion-conduction pore contains an intracellular gate formed by the inner helices, but lacks any extracellular gate in the selectivity filter, as observed in other TRPV channels. Anomalous X-ray diffraction analyses identify a single ion-binding site in the selectivity filter, thus explaining TRPV4 nonselectivity. Structural comparisons with other TRP channels and distantly related voltage-gated cation channels reveal an unprecedented, unique packing interface between the voltage-sensor-like domain and the pore domain, suggesting distinct gating mechanisms. Moreover, our structure begins to provide mechanistic insights to the large set of pathogenic mutations, offering potential opportunities for drug development.

PubMed: 29483651
DOI: 10.1038/s41594-018-0037-5

実験手法

X-RAY DIFFRACTION (6.5 Å)