4H11
Interaction partners of PSD-93 studied by X-ray crystallography and fluorescent polarization spectroscopy
4H11 の概要
エントリーDOI | 10.2210/pdb4h11/pdb |
分子名称 | Disks large homolog 2, SULFATE ION, ACETATE ION, ... (4 entities in total) |
機能のキーワード | all beta pdz, protein interaction, protein binding, neuropeptide |
由来する生物種 | Rattus norvegicus (rat) |
細胞内の位置 | Cell membrane ; Lipid-anchor : Q63622 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 22358.11 |
構造登録者 | |
主引用文献 | Fiorentini, M.,Bach, A.,Stromgaard, K.,Kastrup, J.S.,Gajhede, M. Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy. Acta Crystallogr.,Sect.D, 69:587-594, 2013 Cited by PubMed Abstract: 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. PubMed: 23519667DOI: 10.1107/S0907444912051839 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.67 Å) |
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