1my2: Difference between revisions
New page: left|200px<br /><applet load="1my2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1my2, resolution 1.80Å" /> '''crystal titration ex... |
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[[Image:1my2.jpg|left|200px]]<br /><applet load="1my2" size=" | [[Image:1my2.jpg|left|200px]]<br /><applet load="1my2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1my2, resolution 1.80Å" /> | caption="1my2, resolution 1.80Å" /> | ||
'''crystal titration experiment (AMPA complex control)'''<br /> | '''crystal titration experiment (AMPA complex control)'''<br /> | ||
==Overview== | ==Overview== | ||
An unresolved problem in understanding neurotransmitter receptor function | An unresolved problem in understanding neurotransmitter receptor function concerns the mechanism(s) by which full and partial agonists elicit different amplitude responses at equal receptor occupancy. The widely held view of 'partial agonism' posits that resting and active states of the receptor are in equilibrium, and partial agonists simply do not shift the equilibrium toward the active state as efficaciously as full agonists. Here we report findings from crystallographic and electrophysiological studies of the mechanism of activation of an AMPA-subtype glutamate receptor ion channel. In these experiments, we used 5-substituted willardiines, a series of partial agonists that differ by only a single atom. Our results show that the GluR2 ligand-binding core can adopt a range of ligand-dependent conformational states, which in turn control the open probability of discrete subconductance states of the intact ion channel. Our findings thus provide a structure-based model of partial agonism. | ||
==About this Structure== | ==About this Structure== | ||
1MY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN and AMQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1MY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=AMQ:'>AMQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MY2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: s1s2]] | [[Category: s1s2]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:14 2008'' | ||
Revision as of 15:00, 21 February 2008
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crystal titration experiment (AMPA complex control)
OverviewOverview
An unresolved problem in understanding neurotransmitter receptor function concerns the mechanism(s) by which full and partial agonists elicit different amplitude responses at equal receptor occupancy. The widely held view of 'partial agonism' posits that resting and active states of the receptor are in equilibrium, and partial agonists simply do not shift the equilibrium toward the active state as efficaciously as full agonists. Here we report findings from crystallographic and electrophysiological studies of the mechanism of activation of an AMPA-subtype glutamate receptor ion channel. In these experiments, we used 5-substituted willardiines, a series of partial agonists that differ by only a single atom. Our results show that the GluR2 ligand-binding core can adopt a range of ligand-dependent conformational states, which in turn control the open probability of discrete subconductance states of the intact ion channel. Our findings thus provide a structure-based model of partial agonism.
About this StructureAbout this Structure
1MY2 is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for partial agonist action at ionotropic glutamate receptors., Jin R, Banke TG, Mayer ML, Traynelis SF, Gouaux E, Nat Neurosci. 2003 Aug;6(8):803-10. PMID:12872125
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