6DVZ

Cryo-EM structure of mouse TRPV3-Y564A in complex with 2-Aminoethoxydiphenyl borate (2-APB)

6DVZ の概要

• エントリーDOI: 10.2210/pdb6dvz/pdb
• EMDBエントリー: 8921
• 分子名称: Transient receptor potential cation channel subfamily V member 3, 2-aminoethyl diphenylborinate (2 entities in total)
• 機能のキーワード: trpv3, trp channels, calcium channels, 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: 365162.82

構造登録者

Singh, A.K.,McGoldrick, L.L.,Sobolevsky, A.I. (登録日: 2018-06-25, 公開日: 2018-09-05, 最終更新日: 2024-12-25)

主引用文献

Singh, A.K.,McGoldrick, L.L.,Sobolevsky, A.I.
Structure and gating mechanism of the transient receptor potential channel TRPV3.
Nat. Struct. Mol. Biol., 25:805-813, 2018

PubMed Abstract: Transient receptor potential vanilloid subfamily member 3 (TRPV3) channel plays a crucial role in skin physiology and pathophysiology. Mutations in TRPV3 are associated with various skin diseases, including Olmsted syndrome, atopic dermatitis, and rosacea. Here we present the cryo-electron microscopy structures of full-length mouse TRPV3 in the closed apo and agonist-bound open states. The agonist binds three allosteric sites distal to the pore. Channel opening is accompanied by conformational changes in both the outer pore and the intracellular gate. The gate is formed by the pore-lining S6 helices that undergo local α-to-π helical transitions, elongate, rotate, and splay apart in the open state. In the closed state, the shorter S6 segments are entirely α-helical, expose their nonpolar surfaces to the pore, and hydrophobically seal the ion permeation pathway. These findings further illuminate TRP channel activation and can aid in the design of drugs for the treatment of inflammatory skin conditions, itch, and pain.

PubMed: 30127359
DOI: 10.1038/s41594-018-0108-7

実験手法

ELECTRON MICROSCOPY (4.24 Å)