Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy

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Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy. / Fiorentini, Monica; Bach, Anders; Strømgaard, Kristian; Kastrup, Jette S; Gajhede, Michael.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 69, No. Pt 4, 04.2013, p. 587-94.

Research output: Contribution to journalJournal articleResearch

Harvard

Fiorentini, M, Bach, A, Strømgaard, K, Kastrup, JS & Gajhede, M 2013, 'Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy', Acta Crystallographica. Section D: Biological Crystallography, vol. 69, no. Pt 4, pp. 587-94. https://doi.org/10.1107/S0907444912051839

APA

Fiorentini, M., Bach, A., Strømgaard, K., Kastrup, J. S., & Gajhede, M. (2013). Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy. Acta Crystallographica. Section D: Biological Crystallography, 69(Pt 4), 587-94. https://doi.org/10.1107/S0907444912051839

Vancouver

Fiorentini M, Bach A, Strømgaard K, Kastrup JS, Gajhede M. Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy. Acta Crystallographica. Section D: Biological Crystallography. 2013 Apr;69(Pt 4):587-94. https://doi.org/10.1107/S0907444912051839

Author

Fiorentini, Monica ; Bach, Anders ; Strømgaard, Kristian ; Kastrup, Jette S ; Gajhede, Michael. / Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy. In: Acta Crystallographica. Section D: Biological Crystallography. 2013 ; Vol. 69, No. Pt 4. pp. 587-94.

Bibtex

@article{dbf33b67bbb1423b9e8aa209431c80a8,
title = "Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy",
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.",
keywords = "Cell Communication, Crystallization, Crystallography, X-Ray, Fluorescence Polarization, Guanylate Kinase, Humans, Microscopy, Fluorescence, Multiphoton, Peptide Fragments, Protein Interaction Mapping, Protein Structure, Tertiary, Spectrometry, Fluorescence, Tumor Suppressor Proteins",
author = "Monica Fiorentini and Anders Bach and Kristian Str{\o}mgaard and Kastrup, {Jette S} and Michael Gajhede",
year = "2013",
month = "4",
doi = "10.1107/S0907444912051839",
language = "English",
volume = "69",
pages = "587--94",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 4",

}

RIS

TY - JOUR

T1 - Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy

AU - Fiorentini, Monica

AU - Bach, Anders

AU - Strømgaard, Kristian

AU - Kastrup, Jette S

AU - Gajhede, Michael

PY - 2013/4

Y1 - 2013/4

N2 - 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.

AB - 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.

KW - Cell Communication

KW - Crystallization

KW - Crystallography, X-Ray

KW - Fluorescence Polarization

KW - Guanylate Kinase

KW - Humans

KW - Microscopy, Fluorescence, Multiphoton

KW - Peptide Fragments

KW - Protein Interaction Mapping

KW - Protein Structure, Tertiary

KW - Spectrometry, Fluorescence

KW - Tumor Suppressor Proteins

U2 - 10.1107/S0907444912051839

DO - 10.1107/S0907444912051839

M3 - Journal article

C2 - 23519667

VL - 69

SP - 587

EP - 594

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - Pt 4

ER -

ID: 74768301