1OED

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

1OED の概要

• エントリーDOI: 10.2210/pdb1oed/pdb
• 関連するPDBエントリー: 1ABT 1DXZ 1EQ8 1IDG 1IDH 1LK1 1LXG 1LXH 1TOR 1TOS 3MRA
• EMDBエントリー: 1044
• 分子名称: Acetylcholine receptor subunit alpha, Acetylcholine receptor beta subunit, Acetylcholine receptor delta subunit, ... (4 entities in total)
• 機能のキーワード: ion channel/receptor, ion channel, tubular crystal, acetylcholine receptor, transmembrane, ion channel-receptor complex
• 由来する生物種: Torpedo marmorata (Marbled electric ray); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 137857.90

構造登録者

Miyazawa, A.,Fujiyoshi, Y.,Unwin, N. (登録日: 2003-03-24, 公開日: 2003-06-26, 最終更新日: 2024-05-08)

主引用文献

Miyazawa, A.,Fujiyoshi, Y.,Unwin, N.
Structure and Gating Mechanism of the Acetylcholine Receptor Pore.
Nature, 423:949-, 2003

PubMed Abstract: The nicotinic acetylcholine receptor controls electrical signalling between nerve and muscle cells by opening and closing a gated, membrane-spanning pore. Here we present an atomic model of the closed pore, obtained by electron microscopy of crystalline postsynaptic membranes. The pore is shaped by an inner ring of 5 alpha-helices, which curve radially to create a tapering path for the ions, and an outer ring of 15 alpha-helices, which coil around each other and shield the inner ring from the lipids. The gate is a constricting hydrophobic girdle at the middle of the lipid bilayer, formed by weak interactions between neighbouring inner helices. When acetylcholine enters the ligand-binding domain, it triggers rotations of the protein chains on opposite sides of the entrance to the pore. These rotations are communicated through the inner helices, and open the pore by breaking the girdle apart.

PubMed: 12827192
DOI: 10.1038/NATURE01748

実験手法

ELECTRON MICROSCOPY (4 Å)