{"refrec":{"BRefID":289361,"RR":"<b>Unwin, N.; Fujiyoshi, Y.</b> (2012). Gating movement of acetylcholine receptor caught by plunge-freezing. <i>J. Mol. Biol. 422(5)</i>: 617-634. <a href=\"https://dx.doi.org/10.1016/j.jmb.2012.07.010\" target=\"_blank\">https://dx.doi.org/10.1016/j.jmb.2012.07.010</a>","BEntID":281398,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>J. Mol. Biol. 422(5)</i>: 617-634. <a href=\"https://dx.doi.org/10.1016/j.jmb.2012.07.010\" target=\"_blank\">https://dx.doi.org/10.1016/j.jmb.2012.07.010</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Unwin, N.; Fujiyoshi, Y.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Unwin, N.; Fujiyoshi, Y.","Englishabstract":"The nicotinic acetylcholine (ACh) receptor converts transiently to an open-channel form when activated by ACh released into the synaptic cleft. We describe here the conformational change underlying this event, determined by electron microscopy of ACh-sprayed and freeze-trapped postsynaptic membranes. ACh binding to the alpha subunits triggers a concerted rearrangement in the ligand-binding domain, involving an similar to 1-angstrom outward displacement of the extracellular portion of the beta subunit where it interacts with the juxtaposed ends of alpha-helices shaping the narrow membrane-spanning pore. The beta-subunit helices tilt outward to accommodate this displacement, destabilising the arrangement of pore-lining helices, which in the closed channel bend inward symmetrically to form a central hydrophobic gate. Straightening and tangential motion of the pore-lining helices effect channel opening by widening the pore asymmetrically and increasing its polarity in the region of the gate. The pore-lining helices of the alpha(gamma) and delta subunits, by flexing between alternative bent and straight conformations, undergo the greatest movements. 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