1gr2: Difference between revisions

Revision as of 05:56, 1 July 2008

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File:1gr2.png

Template:STRUCTURE 1gr2

STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATESTRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE

Template:ABSTRACT PUBMED 9804426

About this StructureAbout this Structure

1GR2 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a glutamate-receptor ligand-binding core in complex with kainate., Armstrong N, Sun Y, Chen GQ, Gouaux E, Nature. 1998 Oct 29;395(6705):913-7. PMID:9804426

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 {{STRUCTURE_1gr2|  PDB=1gr2  |  SCENE=  }}
-'''STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE'''
+===STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE===
-==Overview==
+<!--
-Ionotropic glutamate receptors (iGluRs) mediate excitatory synaptic transmission in vertebrates and invertebrates through ligand-induced opening of transmembrane ion channels. iGluRs are segregated into three subtypes according to their sensitivity to the agonists AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid), kainate (a structural analogue of glutamate) or NMDA (N-methyl-D-aspartate). iGluRs are important in the development and function of the nervous system, are essential in memory and learning, and are either implicated in or have causal roles in dysfunctions ranging from Alzheimer's, Parkinson's and Huntington's diseases, schizophrenia, epilepsy and Rasmussen's encephalitis to stroke. Development of iGluR agonists and antagonists has been hampered by a lack of high-resolution structural information. Here we describe the crystal structure of an iGluR ligand-binding region in a complex with the neurotoxin (agonist) kainate. The bilobed structure shows the determinants of receptor-agonist interactions and how ligand-binding specificity and affinity are altered by remote residues and the redox state of the conserved disulphide bond. The structure indicates mechanisms for allosteric effector action and for ligand-induced channel gating. The information provided by this structure will be essential in designing new ligands.
+The line below this paragraph, {{ABSTRACT_PUBMED_9804426}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9804426 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9804426}}
 ==About this Structure==
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 [[Category: Excitory neurotransmitter receptor]]
 [[Category: Glutamate receptor]]
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