1fto: Difference between revisions

Revision as of 03:55, 1 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:1fto.png

Template:STRUCTURE 1fto

CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTIONCRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTION

Template:ABSTRACT PUBMED 11086992

About this StructureAbout this Structure

1FTO is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core., Armstrong N, Gouaux E, Neuron. 2000 Oct;28(1):165-81. PMID:11086992

Page seeded by OCA on Tue Jul 1 03:55:50 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fto.jpg|left|200px]]
+{{Seed}}
+[[Image:1fto.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1fto|  PDB=1fto  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTION'''
+===CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTION===
-==Overview==
+<!--
-Crystal structures of the GluR2 ligand binding core (S1S2) have been determined in the apo state and in the presence of the antagonist DNQX, the partial agonist kainate, and the full agonists AMPA and glutamate. The domains of the S1S2 ligand binding core are expanded in the apo state and contract upon ligand binding with the extent of domain separation decreasing in the order of apo &gt; DNQX &gt; kainate &gt; glutamate approximately equal to AMPA. These results suggest that agonist-induced domain closure gates the transmembrane channel and the extent of receptor activation depends upon the degree of domain closure. AMPA and glutamate also promote a 180 degrees flip of a trans peptide bond in the ligand binding site. The crystal packing of the ligand binding cores suggests modes for subunit-subunit contact in the intact receptor and mechanisms by which allosteric effectors modulate receptor activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_11086992}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11086992 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11086992}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Ligand binding domain]]
 [[Category: Unligandeded]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:45:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:55:50 2008''