1ZOK
PDZ1 Domain Of Synapse Associated Protein 97
Summary for 1ZOK
| Entry DOI | 10.2210/pdb1zok/pdb |
| Descriptor | Presynaptic protein SAP97 (1 entity in total) |
| Functional Keywords | pdz, pdz1, sap97, synapse associated protein 97, beta strand, helix, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Membrane; Peripheral membrane protein (By similarity): Q62696 |
| Total number of polymer chains | 1 |
| Total formula weight | 10089.32 |
| Authors | Wang, L.,Piserchio, A.,Mierke, D.F. (deposition date: 2005-05-13, release date: 2005-06-07, Last modification date: 2024-05-22) |
| Primary citation | Wang, L.,Piserchio, A.,Mierke, D.F. Structural Characterization of the Intermolecular Interactions of Synapse-associated Protein-97 with the NR2B Subunit of N-Methyl-D-aspartate Receptors. J.Biol.Chem., 280:26992-26996, 2005 Cited by PubMed Abstract: The synapse-associated protein-97 (SAP97) is important in the proper trafficking and cell surface maintenance of the N-methyl-D-aspartate ionotropic glutamate receptor. The molecular scaffold/receptor interaction is mediated by the association of the C terminus of the NR2B subunit of the N-methyl-D-aspartate receptor with the PDZ domains of SAP97. Here, we characterize the binding of the C terminus of NR2B with the PDZ domains of SAP97 and determine the structure of the PDZ1-NR2B complex employing high-resolution NMR. Based on fluorescence anisotropy, the NR2B subunit binds to the first and second PDZ domains of SAP97, with higher affinity for PDZ2; no appreciable binding to PDZ3 could be measured. The structural features of the NR2B bound to PDZ1 is consistent with the canonical PDZ-binding motif with the glutamic acid at the -3 position of the C terminus (i.e. -E-S-D-V) interacting with the beta2/beta3 loop. Two sites within the loop of PDZ1 were replaced with the corresponding residue from PDZ2, D243G and P245Q. The former mutation, designed to remove a possible Coulombic repulsion between E(-3)(NR2B) and Asp-243 (PDZ1) has only a minimal effect on binding. The P245Q mutation leads to a 2-fold increase in binding affinity of NR2B, approaching that observed for wild-type PDZ2. These results indicate that modification of the beta2/beta3 loop provides an avenue for regulating the ligand specificity of PDZ domains. PubMed: 15929985DOI: 10.1074/jbc.M503555200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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