6VD7

Cryo-EM structure of Xenopus tropicalis pannexin 1 channel

6VD7 の概要

• エントリーDOI: 10.2210/pdb6vd7/pdb
• EMDBエントリー: 21150
• 分子名称: Pannexin (1 entity in total)
• 機能のキーワード: channel, atp release, heptamer, transport protein
• 由来する生物種: Xenopus tropicalis (Western clawed frog)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 275969.04

構造登録者

Syrjanen, J.L.,Michalski, M.,Furukawa, H.,Kawate, T. (登録日: 2019-12-23, 公開日: 2020-02-26, 最終更新日: 2024-10-23)

主引用文献

Michalski, K.,Syrjanen, J.L.,Henze, E.,Kumpf, J.,Furukawa, H.,Kawate, T.
The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition.
Elife, 9:-, 2020

PubMed Abstract: Pannexins are large-pore forming channels responsible for ATP release under a variety of physiological and pathological conditions. Although predicted to share similar membrane topology with other large-pore forming proteins such as connexins, innexins, and LRRC8, pannexins have minimal sequence similarity to these protein families. Here, we present the cryo-EM structure of a frog pannexin 1 (Panx1) channel at 3.0 Å. We find that Panx1 protomers harbor four transmembrane helices similar in arrangement to other large-pore forming proteins but assemble as a heptameric channel with a unique constriction formed by Trp74 in the first extracellular loop. Mutating Trp74 or the nearby Arg75 disrupt ion selectivity, whereas altering residues in the hydrophobic groove formed by the two extracellular loops abrogates channel inhibition by carbenoxolone. Our structural and functional study establishes the extracellular loops as important structural motifs for ion selectivity and channel inhibition in Panx1.

PubMed: 32048993
DOI: 10.7554/eLife.54670

実験手法

ELECTRON MICROSCOPY (3.02 Å)