1my2
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(New page: 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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Revision as of 19:40, 20 November 2007
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crystal titration experiment (AMPA complex control)
Overview
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
1MY2 is a Single protein structure of sequence from Rattus norvegicus with ZN and AMQ as ligands. Full crystallographic information is available from OCA.
Reference
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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