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http://purl.uniprot.org/citations/22841691http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22841691http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22841691http://www.w3.org/2000/01/rdf-schema#comment"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 α subunits triggers a concerted rearrangement in the ligand-binding domain, involving an ~1-Å outward displacement of the extracellular portion of the β subunit where it interacts with the juxtaposed ends of α-helices shaping the narrow membrane-spanning pore. The β-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 α(γ) and δ subunits, by flexing between alternative bent and straight conformations, undergo the greatest movements. This coupled allosteric transition shifts the structure from a tense (closed) state toward a more relaxed (open) state."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2012.07.010"xsd:string
http://purl.uniprot.org/citations/22841691http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2012.07.010"xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/author"Fujiyoshi Y."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/author"Fujiyoshi Y."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/author"Unwin N."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/author"Unwin N."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/pages"617-634"xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/pages"617-634"xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/title"Gating movement of acetylcholine receptor caught by plunge-freezing."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/title"Gating movement of acetylcholine receptor caught by plunge-freezing."xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/volume"422"xsd:string
http://purl.uniprot.org/citations/22841691http://purl.uniprot.org/core/volume"422"xsd:string
http://purl.uniprot.org/citations/22841691http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22841691
http://purl.uniprot.org/citations/22841691http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22841691
http://purl.uniprot.org/citations/22841691http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22841691
http://purl.uniprot.org/citations/22841691http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22841691
http://purl.uniprot.org/uniprot/Q6S3H9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22841691
http://purl.uniprot.org/uniprot/Q6S3H8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22841691