1oed | pdb_00001oed

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

spinqualitylabelsall models 1oed, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1oed is a 5 chain structure with sequence from Torpedo marmorata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1abt, 1dxz, 1idg, 1idh, 1lk1, 1lxg, 1lxh, 1tor, 1tos, 3mra, 1eq8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACHG_TORCA] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. [ACHA_TORCA] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. [ACHD_TORCA] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. [ACHB_TORCA] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure and gating mechanism of the acetylcholine receptor pore.,Miyazawa A, Fujiyoshi Y, Unwin N Nature. 2003 Jun 26;423(6943):949-55. PMID:12827192 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nicotinic Acetylcholine Receptor

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