6LGP

cryo-EM structure of TRPV3 in lipid nanodisc

6LGP の概要

• エントリーDOI: 10.2210/pdb6lgp/pdb
• EMDBエントリー: 0882
• 分子名称: Transient receptor potential cation channel subfamily V member 3, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, DIUNDECYL PHOSPHATIDYL CHOLINE (3 entities in total)
• 機能のキーワード: trp channel, trpv family, trpv3, nanodisc, membrane protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 315434.69

構造登録者

Shimada, H.,Kusakizako, T.,Nishizawa, T.,Nureki, O. (登録日: 2019-12-05, 公開日: 2020-06-24, 最終更新日: 2025-06-25)

主引用文献

Shimada, H.,Kusakizako, T.,Dung Nguyen, T.H.,Nishizawa, T.,Hino, T.,Tominaga, M.,Nureki, O.
The structure of lipid nanodisc-reconstituted TRPV3 reveals the gating mechanism.
Nat.Struct.Mol.Biol., 27:645-652, 2020

PubMed Abstract: 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 physiological lipids are involved in the TRPV3 activation. Here we determined the apo state structure of mouse (Mus musculus) TRPV3 in a lipid nanodisc at 3.3 Å resolution. The structure revealed that lipids bound to the pore domain stabilize the selectivity filter in the narrow state, suggesting that the selectivity filter of TRPV3 affects cation permeation. When the lower gate is closed in nanodisc-reconstituted TRPV3, the S6 helix adopts the π-helical conformation without agonist- or heat-sensitization, potentially stabilized by putative intra-subunit hydrogen bonds and lipid binding. Our findings provide insights into the lipid-associated gating mechanism of TRPV3.

PubMed: 32572254
DOI: 10.1038/s41594-020-0439-z

実験手法

ELECTRON MICROSCOPY (3.3 Å)