4aq5
From Proteopedia
(Difference between revisions)
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| - | + | ==Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class)== | |
| - | + | <StructureSection load='4aq5' size='340' side='right' caption='[[4aq5]], [[Resolution|resolution]] 6.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4aq5]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AQ5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l4w|1l4w]], [[1ljz|1ljz]], [[1oed|1oed]], [[2bg9|2bg9]], [[4aq9|4aq9]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aq5 RCSB], [http://www.ebi.ac.uk/pdbsum/4aq5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 ~1-A 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. This coupled allosteric transition shifts the structure from a tense (closed) state toward a more relaxed (open) state. | ||
| - | + | Gating movement of acetylcholine receptor caught by plunge-freezing.,Unwin N, Fujiyoshi Y J Mol Biol. 2012 Oct 5;422(5):617-34. Epub 2012 Jul 24. PMID:22841691<ref>PMID:22841691</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Torpedo marmorata]] | [[Category: Torpedo marmorata]] | ||
| - | [[Category: Fujiyoshi, Y | + | [[Category: Fujiyoshi, Y]] |
| - | [[Category: Unwin, N | + | [[Category: Unwin, N]] |
[[Category: Allosteric mechanism]] | [[Category: Allosteric mechanism]] | ||
[[Category: Asymmetric gating]] | [[Category: Asymmetric gating]] | ||
[[Category: Freeze-trapping]] | [[Category: Freeze-trapping]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 10:01, 21 December 2014
Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class)
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