1gr2

From Proteopedia

Revision as of 14:07, 20 November 2007

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.

About this Structure

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

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:9804426

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