9OQP

Human pannexin 1 channel with 1mM mefloquine

これはPDB形式変換不可エントリーです。

9OQP の概要

• エントリーDOI: 10.2210/pdb9oqp/pdb
• EMDBエントリー: 70769
• 分子名称: Pannexin-1,RNA-directed RNA polymerase L, (11S,12R)-Mefloquine (2 entities in total)
• 機能のキーワード: pannexin 1 channel with mefloquine, transport protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 548658.96

構造登録者

Ruan, Z.,Li, Y.,Du, J.,Lu, W. (登録日: 2025-05-21, 公開日: 2025-12-24)

主引用文献

Li, Y.,Ruan, Z.,Lee, J.,Orozco, I.J.,Zhou, E.,Du, J.,Lu, W.
Structural basis of PANX1 permeation and positive modulation by mefloquine.
Nat Commun, 16:11057-11057, 2025

PubMed Abstract: Purinergic signaling relies on ATP release through exocytosis and large-pore channels. Large-pore channels permeate both small anions like chloride and large signaling molecules like ATP, but how this broad cargo selectivity is structurally controlled remains elusive. Here we investigate PANX1, a prototypical large-pore channel, and uncover structural plasticity at the extracellular entrance formed by seven tryptophan (W74) residues. The W74 sidechains are flexible, sampling conformations that range from a constricted state permissive only to chloride to a dilated state compatible with ATP. These states are coupled to variable cation-π interactions between W74 and arginine 75 (R75), suggesting a mechanism for dynamic tuning of pore architecture and selective cargo permeation. We also identify mefloquine as a positive modulator of PANX1 that binds near the side tunnel to control ion flow through this pathway. Together, these findings define the structural principles underlying PANX1 permeation and modulation.

PubMed: 41381453
DOI: 10.1038/s41467-025-66028-9

実験手法

ELECTRON MICROSCOPY (2.62 Å)