1ewt

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Revision as of 12:15, 20 November 2007

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spinqualitylabelsall models 1ewt, resolution 3.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF METABOTROPIC GLUTAMATE RECEPTOR SUBTYPE 1 LIGAND FREE FORM I

Overview

The metabotropic glutamate receptors (mGluRs) are key receptors in the, modulation of excitatory synaptic transmission in the central nervous, system. Here we have determined three different crystal structures of the, extracellular ligand-binding region of mGluR1--in a complex with glutamate, and in two unliganded forms. They all showed disulphide-linked homodimers, whose 'active' and 'resting' conformations are modulated through the, dimeric interface by a packed alpha-helical structure. The bi-lobed, protomer architectures flexibly change their domain arrangements to form, an 'open' or 'closed' conformation. The structures imply that glutamate, binding stabilizes both the 'active' dimer and the 'closed' protomer in, dynamic equilibrium. Movements of the four domains in the dimer are likely, to affect the separation of the transmembrane and intracellular regions, and thereby activate the receptor. This scheme in the initial receptor, activation could be applied generally to G-protein-coupled, neurotransmitter receptors that possess extracellular ligand-binding, sites.

About this Structure

1EWT is a Single protein structure of sequence from Rattus norvegicus with NAG and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor., Kunishima N, Shimada Y, Tsuji Y, Sato T, Yamamoto M, Kumasaka T, Nakanishi S, Jingami H, Morikawa K, Nature. 2000 Oct 26;407(6807):971-7. PMID:11069170

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