1OED

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

Summary for 1OED

• Entry DOI: 10.2210/pdb1oed/pdb
• Related: 1ABT 1DXZ 1EQ8 1IDG 1IDH 1LK1 1LXG 1LXH 1TOR 1TOS 3MRA
• EMDB information: 1044
• Descriptor: Acetylcholine receptor subunit alpha, Acetylcholine receptor beta subunit, Acetylcholine receptor delta subunit, ... (4 entities in total)
• Functional Keywords: ion channel/receptor, ion channel, tubular crystal, acetylcholine receptor, transmembrane, ion channel-receptor complex
• Biological source: Torpedo marmorata (Marbled electric ray); More
• Total number of polymer chains: 5
• Total formula weight: 137857.90

Authors

Miyazawa, A.,Fujiyoshi, Y.,Unwin, N. (deposition date: 2003-03-24, release date: 2003-06-26, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (4 Å)