1mxw: Difference between revisions

Revision as of 15:25, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mxw.png

Template:STRUCTURE 1mxw

crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW)crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW)

Template:ABSTRACT PUBMED 12872125

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

Page seeded by OCA on Sun Jul 27 15:25:05 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1mxw.gif|left|200px]]
+{{Seed}}
+[[Image:1mxw.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1mxw|  PDB=1mxw  |  SCENE=  }}
-'''crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW)'''
+===crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW)===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12872125}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12872125 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12872125}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Partial agonist]]
 [[Category: S1s2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:51:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:25:05 2008''