4h11
Interaction partners of PSD-93 studied by X-ray crystallography and fluorescent polarization spectroscopyInteraction partners of PSD-93 studied by X-ray crystallography and fluorescent polarization spectroscopy
Structural highlights
Function[DLG2_RAT] Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses (By similarity). Publication Abstract from PubMedPSD-93 (chapsyn-110, DLG2) is a member of the family of membrane-associated guanylate kinase (MAGUK) proteins. The MAGUK proteins are involved in receptor localization and signalling pathways. The best characterized MAGUK protein, PSD-95, is known to be involved in NMDA receptor signalling via its PDZ domains. The PDZ domains of PSD-95 and PSD-93 are structurally very similar, but relatively little is known about the function of PSD-93. PSD-93 has been suggested to interact with GluD2 from the family of ionotropic glutamate receptors. Here, the interactions of four residues (GTSI) representing the extreme C-terminus of GluD2 with PSD-93 PDZ1 have been investigated in the crystalline phase. Two different binding modes of these residues were observed, suggesting that the peptide is not tightly bound to PSD-93 PDZ1. In accordance, the two N-terminal PSD-93 PDZ domains show no appreciable binding affinity for a GluD2-derived C-terminal octapeptide, whereas micromolar affinity was observed for a GluN2B-derived C-terminal octapeptide. This indicates that if present, the interactions between GluD2 and PSD-93 involve more than the extreme terminus of the receptor. In contrast, the tumour-suppressor protein SCRIB PDZ3 shows low micromolar affinity towards the GluD2-derived octapeptide, which is in agreement with previous findings using high-throughput assays. Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy.,Fiorentini M, Bach A, Stromgaard K, Kastrup JS, Gajhede M Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):587-94. doi:, 10.1107/S0907444912051839. Epub 2013 Mar 14. PMID:23519667[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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