1iss

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[[Image:1iss.jpg|left|200px]]
[[Image:1iss.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1iss", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=MCG:(S)-(ALPHA)-METHYL-4-CARBOXYPHENYLGLYCINE'>MCG</scene>
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{{STRUCTURE_1iss| PDB=1iss | SCENE= }}
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|RELATEDENTRY=[[1ewk|1EWK]], [[1ewt|1EWT]], [[1ewv|1EWV]], [[1isr|1ISR]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iss OCA], [http://www.ebi.ac.uk/pdbsum/1iss PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iss RCSB]</span>
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'''Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with an antagonist'''
'''Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with an antagonist'''
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[[Category: Tsuchiya, D.]]
[[Category: Tsuchiya, D.]]
[[Category: 4-carboxyphenylglycine]]
[[Category: 4-carboxyphenylglycine]]
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[[Category: antagonist]]
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[[Category: Antagonist]]
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[[Category: g protein coupled receptor]]
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[[Category: G protein coupled receptor]]
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[[Category: neurotransmitter]]
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[[Category: Neurotransmitter]]
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[[Category: signal transduction]]
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[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:22:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:24:10 2008''
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Revision as of 17:22, 2 May 2008

Template:STRUCTURE 1iss

Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with an antagonist


Overview

Crystal structures of the extracellular ligand-binding region of the metabotropic glutamate receptor, complexed with an antagonist, (S)-(alpha)-methyl-4-carboxyphenylglycine, and with both glutamate and Gd3+ ion, have been determined by x-ray crystallographic analyses. The structure of the complex with the antagonist is similar to that of the unliganded resting dimer. The antagonist wedges the protomer to maintain an inactive open form. The glutamate/Gd3+ complex is an exact 2-fold symmetric dimer, where each bi-lobed protomer adopts the closed conformation. The surface of the C-terminal domain contains an acidic patch, whose negative charges are alleviated by the metal cation to stabilize the active dimeric structure. The structural comparison between the active and resting dimers suggests that glutamate binding tends to induce domain closing and a small shift of a helix in the dimer interface. Furthermore, an interprotomer contact including the acidic patch inhibited dimer formation by the two open protomers in the active state. These findings provide a structural basis to describe the link between ligand binding and the dimer interface.

About this Structure

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

Reference

Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+., Tsuchiya D, Kunishima N, Kamiya N, Jingami H, Morikawa K, Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2660-5. Epub 2002 Feb 26. PMID:11867751 Page seeded by OCA on Fri May 2 20:22:14 2008

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