3rqw: Difference between revisions
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==Crystal structure of acetylcholine bound to a prokaryotic pentameric ligand-gated ion channel, ELIC== | ==Crystal structure of acetylcholine bound to a prokaryotic pentameric ligand-gated ion channel, ELIC== | ||
<StructureSection load='3rqw' size='340' side='right' caption='[[3rqw]], [[Resolution|resolution]] 2.91Å' scene=''> | <StructureSection load='3rqw' size='340' side='right'caption='[[3rqw]], [[Resolution|resolution]] 2.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rqw]] is a 10 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3rqw]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Dicd3 Dicd3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RQW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACH:ACETYLCHOLINE'>ACH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACH:ACETYLCHOLINE'>ACH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rqu|3rqu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rqu|3rqu]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dda3937_00520 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dda3937_00520 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=198628 DICD3])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rqw OCA], [https://pdbe.org/3rqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rqw RCSB], [https://www.ebi.ac.uk/pdbsum/3rqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rqw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Ion channels|Ion channels]] | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Dicd3]] | [[Category: Dicd3]] | ||
[[Category: Large Structures]] | |||
[[Category: Chen, Q]] | [[Category: Chen, Q]] | ||
[[Category: Cohen, A]] | [[Category: Cohen, A]] | ||
Revision as of 13:22, 22 June 2022
Crystal structure of acetylcholine bound to a prokaryotic pentameric ligand-gated ion channel, ELICCrystal structure of acetylcholine bound to a prokaryotic pentameric ligand-gated ion channel, ELIC
Structural highlights
Publication Abstract from PubMedELIC, the pentameric ligand-gated ion channel from Erwinia chrysanthemi, is a prototype for Cys-loop receptors. Here we show that acetylcholine is a competitive antagonist for ELIC. We determine the acetylcholine-ELIC cocrystal structure to a 2.9-A resolution and find that acetylcholine binding to an aromatic cage at the subunit interface induces a significant contraction of loop C and other structural rearrangements in the extracellular domain. The side chain of the pore-lining residue F247 reorients and the pore size consequently enlarges, but the channel remains closed. We attribute the inability of acetylcholine to activate ELIC primarily to weak cation-pi and electrostatic interactions in the pocket, because an acetylcholine derivative with a simple quaternary-to-tertiary ammonium substitution activates the channel. This study presents a compelling case for understanding the structural underpinning of the functional relationship between agonism and competitive antagonism in the Cys-loop receptors, providing a new framework for developing novel therapeutic drugs. Structure of the pentameric ligand-gated ion channel ELIC cocrystallized with its competitive antagonist acetylcholine.,Pan J, Chen Q, Willenbring D, Yoshida K, Tillman T, Kashlan OB, Cohen A, Kong XP, Xu Y, Tang P Nat Commun. 2012 Mar 6;3:714. doi: 10.1038/ncomms1703. PMID:22395605[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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