6D73

Cryo-EM structure of the zebrafish TRPM2 channel in the presence of Ca2+

6D73 の概要

• エントリーDOI: 10.2210/pdb6d73/pdb
• EMDBエントリー: 7822
• 分子名称: Transient receptor potential cation channel, subfamily M, CALCIUM ION (2 entities in total)
• 機能のキーワード: warmth sensor, redox sensor, calcium-permeable ion channel, ion channel, transport protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 670594.81

構造登録者

Yin, Y.,Wu, M.,Borschel, W.F.,Lander, G.C.,Lee, S.-Y. (登録日: 2018-04-23, 公開日: 2019-05-15, 最終更新日: 2024-11-06)

主引用文献

Yin, Y.,Wu, M.,Hsu, A.L.,Borschel, W.F.,Borgnia, M.J.,Lander, G.C.,Lee, S.Y.
Visualizing structural transitions of ligand-dependent gating of the TRPM2 channel.
Nat Commun, 10:3740-3740, 2019

PubMed Abstract: The transient receptor potential melastatin 2 (TRPM2) channel plays a key role in redox sensation in many cell types. Channel activation requires binding of both ADP-ribose (ADPR) and Ca. The recently published TRPM2 structures from Danio rerio in the ligand-free and the ADPR/Ca-bound conditions represent the channel in closed and open states, which uncovered substantial tertiary and quaternary conformational rearrangements. However, it is unclear how these rearrangements are achieved within the tetrameric channel during channel gating. Here we report the cryo-electron microscopy structures of Danio rerio TRPM2 in the absence of ligands, in complex with Ca alone, and with both ADPR and Ca, resolved to ~4.3 Å, ~3.8 Å, and ~4.2 Å, respectively. In contrast to the published results, our studies capture ligand-bound TRPM2 structures in two-fold symmetric intermediate states, offering a glimpse of the structural transitions that bridge the closed and open conformations.

PubMed: 31431622
DOI: 10.1038/s41467-019-11733-5

実験手法

ELECTRON MICROSCOPY (3.8 Å)