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PDBsum entry 4h11
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References listed in PDB file
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Key reference
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Title
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Interaction partners of psd-93 studied by X-Ray crystallography and fluorescence polarization spectroscopy.
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Authors
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M.Fiorentini,
A.Bach,
K.Strømgaard,
J.S.Kastrup,
M.Gajhede.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2013,
69,
587-594.
[DOI no: ]
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PubMed id
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Abstract
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PSD-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.
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