1gr2: Difference between revisions
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[[Image:1gr2.jpg|left|200px]] | [[Image:1gr2.jpg|left|200px]] | ||
'''STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE''' | {{Structure | ||
|PDB= 1gr2 |SIZE=350|CAPTION= <scene name='initialview01'>1gr2</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=KAI:3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE'>KAI</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GR2 is a [ | 1GR2 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=1GR2 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9804426 9804426] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: glutamate receptor]] | [[Category: glutamate receptor]] | ||
''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 11:26:52 2008'' | ||
Revision as of 12:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE
OverviewOverview
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.
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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