1my2: Difference between revisions
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|PDB= 1my2 |SIZE=350|CAPTION= <scene name='initialview01'>1my2</scene>, resolution 1.80Å | |PDB= 1my2 |SIZE=350|CAPTION= <scene name='initialview01'>1my2</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=AMQ:(S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC+ACID'>AMQ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ftm|1FTM]], [[1mxu|1MXU]], [[1mxv|1MXV]], [[1mxw|1MXW]], [[1mxx|1MXX]], [[1mxy|1MXY]], [[1mxz|1MXZ]], [[1my0|1MY0]], [[1my1|1MY1]], [[1my3|1MY3]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1my2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1my2 OCA], [http://www.ebi.ac.uk/pdbsum/1my2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1my2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Gouaux, E.]] | [[Category: Gouaux, E.]] | ||
[[Category: Jin, R.]] | [[Category: Jin, R.]] | ||
[[Category: ampa]] | [[Category: ampa]] | ||
[[Category: bromo-willardiine]] | [[Category: bromo-willardiine]] | ||
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[[Category: s1s2]] | [[Category: s1s2]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:45 2008'' | ||
Revision as of 22:22, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1FTM, 1MXU, 1MXV, 1MXW, 1MXX, 1MXY, 1MXZ, 1MY0, 1MY1, 1MY3
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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