1JXM
CRYSTAL STRUCTURE OF THE GMP BOUND SH3-HOOK-GK FRAGMENT OF PSD-95
Summary for 1JXM
| Entry DOI | 10.2210/pdb1jxm/pdb |
| Related | 1JXO |
| Descriptor | POSTSYNAPTIC DENSITY PROTEIN, GUANOSINE-5'-MONOPHOSPHATE, GUANIDINE, ... (5 entities in total) |
| Functional Keywords | maguk, postsynaptic density, sh3 domain, guanylate kinase domain, structural protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cell membrane; Peripheral membrane protein: P31016 |
| Total number of polymer chains | 1 |
| Total formula weight | 35530.70 |
| Authors | Tavares, G.A.,Panepucci, E.H.,Brunger, A.T. (deposition date: 2001-09-07, release date: 2002-01-16, Last modification date: 2023-11-29) |
| Primary citation | Tavares, G.A.,Panepucci, E.H.,Brunger, A.T. Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95. Mol.Cell, 8:1313-1325, 2001 Cited by PubMed Abstract: PSD-95/SAP90 is a member of the MAGUK superfamily. In excitatory synapses, PSD-95 clusters receptors and ion channels at specific sites in the postsynaptic membrane and organizes downstream signaling and cytoskeletal molecules. We have determined the crystal structures of the apo and GMP-bound forms to 2.3 and 2.0 A resolutions, respectively, of a fragment containing the SH3, HOOK, and guanylate kinase (GK) domains of PSD-95. We observe an intramolecular interaction between the SH3 and GK domains involving the formation of a beta sheet including residues N- and C-terminal to the GK domain. Based on amino acid conservation and mutational data available in the literature, we propose that this intramolecular interaction is a common feature among MAGUK proteins. PubMed: 11779506DOI: 10.1016/S1097-2765(01)00416-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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