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1JXO

Crystal Structure of the SH3-HOOK-GK Fragment of PSD-95

Summary for 1JXO
Entry DOI10.2210/pdb1jxo/pdb
Related1JXM
Descriptorpostsynaptic density protein (2 entities in total)
Functional Keywordsmaguk, postsynaptic density, sh3 domain, guanylate kinase domain, structural protein
Biological sourceRattus norvegicus (Norway rat)
Cellular locationCell membrane; Peripheral membrane protein: P31016
Total number of polymer chains2
Total formula weight69625.99
Authors
Tavares, G.A.,Panepucci, E.H.,Brunger, A.T. (deposition date: 2001-09-07, release date: 2002-01-16, Last modification date: 2023-08-16)
Primary citationTavares, 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: 11779506
DOI: 10.1016/S1097-2765(01)00416-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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