1ewt
From Proteopedia
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|PDB= 1ewt |SIZE=350|CAPTION= <scene name='initialview01'>1ewt</scene>, resolution 3.7Å | |PDB= 1ewt |SIZE=350|CAPTION= <scene name='initialview01'>1ewt</scene>, resolution 3.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ewk|1EWK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ewt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ewt OCA], [http://www.ebi.ac.uk/pdbsum/1ewt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ewt RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Shimada, Y.]] | [[Category: Shimada, Y.]] | ||
[[Category: Tsuji, Y.]] | [[Category: Tsuji, Y.]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: SO4]] | ||
[[Category: cn]] | [[Category: cn]] | ||
[[Category: neuron]] | [[Category: neuron]] | ||
| Line 34: | Line 35: | ||
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:11:12 2008'' |
Revision as of 17:11, 30 March 2008
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| , resolution 3.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1EWK
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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