1m5z
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(New page: 200px<br /><applet load="1m5z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5z" /> '''The PDZ7 of Glutamate Receptor Interacting P...)
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Revision as of 19:03, 20 November 2007
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The PDZ7 of Glutamate Receptor Interacting Protein Binds to its Target via a Novel Hydrophobic Surface Area
Overview
Glutamate receptor interacting protein 1 (GRIP1) is a scaffold protein, composed of seven PDZ (Postsynaptic synaptic density-95/Discs large/Zona, occludens-1) domains. The protein plays important roles in the synaptic, targeting of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid, (AMPA) receptors. The interaction between GRIP1 PDZ7 and a Ras guanine, nucleotide exchange factor, GRASP-1, regulates synaptic distribution of, AMPA receptors. Here, we describe the three-dimensional structure of GRIP1, PDZ7 determined by NMR spectroscopy. GRIP1 PDZ7 contains a closed carboxyl, group-binding pocket and a narrow alphaB/betaB-groove that is not likely, to bind to classical PDZ ligands. Unexpectedly, GRIP1 PDZ7 contains a, large solvent-exposed hydrophobic surface at a site distinct from the, conventional ligand-binding alphaB/betaB-groove. NMR titration experiments, show that GRIP1 PDZ7 binds to GRASP-1 via this hydrophobic surface. Our, data uncover a novel PDZ domain-mediated protein interaction mode that may, be responsible for multimerization of other PDZ domain-containing scaffold, proteins.
About this Structure
1M5Z is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
PDZ7 of glutamate receptor interacting protein binds to its target via a novel hydrophobic surface area., Feng W, Fan JS, Jiang M, Shi YW, Zhang M, J Biol Chem. 2002 Oct 25;277(43):41140-6. Epub 2002 Aug 23. PMID:12196542
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