1M5Z
The PDZ7 of Glutamate Receptor Interacting Protein Binds to its Target via a Novel Hydrophobic Surface Area
Summary for 1M5Z
| Entry DOI | 10.2210/pdb1m5z/pdb |
| NMR Information | BMRB: 5499 |
| Descriptor | AMPA receptor interacting protein (1 entity in total) |
| Functional Keywords | six beta-strands and two alpha-helices, protein binding |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasm: P97879 |
| Total number of polymer chains | 1 |
| Total formula weight | 9979.45 |
| Authors | |
| Primary citation | Feng, W.,Fan, J.-S.,Jiang, M.,Shi, Y.-W.,Zhang, M. The PDZ7 of Glutamate Receptor Interacting Protein Binds to its Target via a Novel Hydrophobic Surface Area J.Biol.Chem., 277:41140-41146, 2002 Cited by PubMed Abstract: 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. PubMed: 12196542DOI: 10.1074/jbc.M207206200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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