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| Line 3: |
Line 3: |
| | <SX load='4aq5' size='340' side='right' viewer='molstar' caption='[[4aq5]], [[Resolution|resolution]] 6.20Å' scene=''> | | <SX load='4aq5' size='340' side='right' viewer='molstar' caption='[[4aq5]], [[Resolution|resolution]] 6.20Å' scene=''> |
| | == Structural highlights == | | == 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://proteopedia.org/fgij/fg.htm?mol=4AQ5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4aq5]] is a 5 chain structure with sequence from [https://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 [https://proteopedia.org/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> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l4w|1l4w]], [[1ljz|1ljz]], [[1oed|1oed]], [[2bg9|2bg9]], [[4aq9|4aq9]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aq5 OCA], [http://pdbe.org/4aq5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4aq5 RCSB], [http://www.ebi.ac.uk/pdbsum/4aq5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4aq5 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aq5 OCA], [https://pdbe.org/4aq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aq5 RCSB], [https://www.ebi.ac.uk/pdbsum/4aq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aq5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACHA_TORMA ACHA_TORMA]] 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. | + | [[https://www.uniprot.org/uniprot/ACHA_TORMA ACHA_TORMA]] 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
Function
[ACHA_TORMA] 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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Unwin N, Fujiyoshi Y. Gating movement of acetylcholine receptor caught by plunge-freezing. J Mol Biol. 2012 Oct 5;422(5):617-34. Epub 2012 Jul 24. PMID:22841691 doi:10.1016/j.jmb.2012.07.010
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