9E3F

Torpedo muscle-type nicotinic acetylcholine receptor - Unliganded State

9E3F の概要

• エントリーDOI: 10.2210/pdb9e3f/pdb
• EMDBエントリー: 47481
• 分子名称: Acetylcholine receptor subunit alpha, Acetylcholine receptor subunit beta, Acetylcholine receptor subunit delta, ... (9 entities in total)
• 機能のキーワード: nicotinic acetylcholine receptor, ion channel, cys-loop receptor, pentameric ligand-gated ion channel, neurotransmitter-gated receptor, ligand-gated ion channel, primed state, membrane protein
• 由来する生物種: Tetronarce californica (Pacific electric ray); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 281167.46

構造登録者

Thompson, M.J.,Nury, H.,Zarkadas, E.,Baenziger, J.E. (登録日: 2024-10-23, 公開日: 2025-10-08, 最終更新日: 2026-01-14)

主引用文献

Thompson, M.J.,Tessier, C.J.G.,Ananchenko, A.,Henault, C.,Emlaw, J.R.,Dehez, F.,Zarkadas, E.,daCosta, C.J.B.,Nury, H.,Baenziger, J.E.
Asynchronous subunit transitions prime acetylcholine receptor activation.
Science, 391:eadw1264-eadw1264, 2026

PubMed Abstract: Communication at synapses is facilitated by postsynaptic receptors, which convert a chemical signal into an electrical response. For ligand-gated ion channels, agonist binding triggers rapid transitions through intermediate states leading to a transient open-pore conformation, with these transitions shaping the post-synaptic response. Here, we determine structures of the muscle-type nicotinic acetylcholine receptor in unliganded, mono-liganded, and di-liganded states. Agonist binding to a single site stabilizes a closed structure where an entire principal agonist-binding subunit transitions to an active-like conformation, while the other unoccupied principal subunit remains inactive, albeit poised for activation. Uniting this intermediate structure with single-channel recordings informs a sequential activation mechanism where asynchronous subunit transitions prime the receptor for activation, a finding with implications for an entire superfamily of pentameric ligand-gated ion channels.

PubMed: 41037590
DOI: 10.1126/science.adw1264

実験手法

ELECTRON MICROSCOPY (3.2 Å)