1mqh
From Proteopedia
(New page: 200px<br /><applet load="1mqh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqh, resolution 1.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:1mqh.jpg|left|200px]]<br /><applet load="1mqh" size=" | + | [[Image:1mqh.jpg|left|200px]]<br /><applet load="1mqh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mqh, resolution 1.80Å" /> | caption="1mqh, resolution 1.80Å" /> | ||
'''Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Bromo-Willardiine at 1.8 Angstroms Resolution'''<br /> | '''Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Bromo-Willardiine at 1.8 Angstroms Resolution'''<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== | ||
| - | 1MQH 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 BWD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MQH 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=BWD:'>BWD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Banke, T | + | [[Category: Banke, T G.]] |
[[Category: Gouaux, E.]] | [[Category: Gouaux, E.]] | ||
[[Category: Jin, R.]] | [[Category: Jin, R.]] | ||
| - | [[Category: Mayer, M | + | [[Category: Mayer, M L.]] |
| - | [[Category: Traynelis, S | + | [[Category: Traynelis, S F.]] |
[[Category: BWD]] | [[Category: BWD]] | ||
[[Category: bromo-willardiine]] | [[Category: bromo-willardiine]] | ||
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[[Category: willardiines]] | [[Category: willardiines]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:58 2008'' |
Revision as of 11:57, 21 February 2008
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Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Bromo-Willardiine at 1.8 Angstroms Resolution
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
1MQH is a Single protein structure of sequence from Rattus norvegicus with as ligand. 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
Page seeded by OCA on Thu Feb 21 13:57:58 2008
