6UW8

Cryo-EM structure of the human TRPV3 K169A mutant briefly exposed to 2-APB for 3 minutes, determined in lipid nanodisc

6UW8 の概要

• エントリーDOI: 10.2210/pdb6uw8/pdb
• EMDBエントリー: 20919
• 分子名称: Transient receptor potential cation channel subfamily V member 3 (1 entity in total)
• 機能のキーワード: ion channel trpv3, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 362682.75

構造登録者

Deng, Z.,Yuan, P. (登録日: 2019-11-04, 公開日: 2020-07-01, 最終更新日: 2024-03-06)

主引用文献

Deng, Z.,Maksaev, G.,Rau, M.,Xie, Z.,Hu, H.,Fitzpatrick, J.A.J.,Yuan, P.
Gating of human TRPV3 in a lipid bilayer.
Nat.Struct.Mol.Biol., 27:635-644, 2020

PubMed Abstract: The transient receptor potential cation channel subfamily V member 3 (TRPV3) channel plays a critical role in skin physiology, and mutations in TRPV3 result in the development of a congenital skin disorder, Olmsted syndrome. Here we describe multiple cryo-electron microscopy structures of human TRPV3 reconstituted into lipid nanodiscs, representing distinct functional states during the gating cycle. The ligand-free, closed conformation reveals well-ordered lipids interacting with the channel and two physical constrictions along the ion-conduction pore involving both the extracellular selectivity filter and intracellular helix bundle crossing. Both the selectivity filter and bundle crossing expand upon activation, accompanied by substantial structural rearrangements at the cytoplasmic intersubunit interface. Transition to the inactivated state involves a secondary structure change of the pore-lining helix, which contains a π-helical segment in the closed and open conformations, but becomes entirely α-helical upon inactivation. Together with electrophysiological characterization, structures of TRPV3 in a lipid membrane environment provide unique insights into channel activation and inactivation mechanisms.

PubMed: 32572252
DOI: 10.1038/s41594-020-0428-2

実験手法

ELECTRON MICROSCOPY (4.02 Å)