1m5z

<StructureSection load='1m5z' size='340' side='right'caption='[[1m5z]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1m5z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M5Z FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5z OCA], [https://pdbe.org/1m5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m5z RCSB], [https://www.ebi.ac.uk/pdbsum/1m5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5z ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/GRIP1_RAT GRIP1_RAT]] May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons.<ref>PMID:9069286</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12196542</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m5z" style="background-color:#fffaf0;"></div>

[[Category: Buffalo rat]]

[[Category: Fan, J]]

[[Category: Feng, W]]

[[Category: Jiang, M]]

[[Category: Shi, Y]]

[[Category: Zhang, M]]

[[Category: Six beta-strands and two alpha-helice]]