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1iss
From Proteopedia
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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 with MCG as ligand. 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 Tue Nov 20 17:38:46 2007
