The structure of lipid nanodisc-reconstituted TRPV3 reveals the gating mechanism

Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how p...

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Vydané v:	Nature structural & molecular biology Ročník 27; číslo 7; s. 645 - 652
Hlavní autori:	Shimada, Hiroto, Kusakizako, Tsukasa, Dung Nguyen, T H, Nishizawa, Tomohiro, Hino, Tomoya, Tominaga, Makoto, Nureki, Osamu
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States Nature Publishing Group 01.07.2020
Predmet:	Cations Channel gating Conformation Cryoelectron Microscopy Domains Hydrogen Bonding Hydrogen bonds Ion Channel Gating - physiology Ion channels Ions Lipids Lipids - chemistry Micelles Models, Molecular Nanostructures - chemistry Protein Conformation Selectivity Transient receptor potential proteins TRPV Cation Channels - chemistry TRPV Cation Channels - metabolism
ISSN:	1545-9993, 1545-9985, 1545-9985
On-line prístup:	Získať plný text
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