1mxw: Difference between revisions
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[[Image:1mxw.gif|left|200px]] | [[Image:1mxw.gif|left|200px]] | ||
'''crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW)''' | {{Structure | ||
|PDB= 1mxw |SIZE=350|CAPTION= <scene name='initialview01'>1mxw</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MXW is a [ | 1MXW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXW OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12872125 12872125] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: s1s2]] | [[Category: s1s2]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:37 2008'' | ||
Revision as of 13:49, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW)
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
1MXW 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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