5AN8

Cryo-electron microscopy structure of rabbit TRPV2 ion channel

5AN8 の概要

• エントリーDOI: 10.2210/pdb5an8/pdb
• EMDBエントリー: 6455
• 分子名称: TRPV2 (1 entity in total)
• 機能のキーワード: transport protein, trp channel
• 由来する生物種: ORYCTOLAGUS CUNICULUS (RABBIT)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 279625.56

構造登録者

Zubcevic, L.,Herzik, M.A.J.,Chung, B.C.,Lander, G.C.,Lee, S.Y. (登録日: 2015-09-04, 公開日: 2015-12-23, 最終更新日: 2024-10-16)

主引用文献

Zubcevic, L.,Herzik, M.,Chung, B.C.,Lander, G.C.,Lee, S.Y.
Cryo-Electron Microscopy of the Trpv2 Ion Channel
Nat.Struct.Mol.Biol., 23:180-, 2016

PubMed Abstract: Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ∼4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.

PubMed: 26779611
DOI: 10.1038/NSMB.3159

実験手法

ELECTRON MICROSCOPY (3.8 Å)