The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligandCitation formats

  • External authors:
  • Nazahiyah Rodzli
  • C W Levy
  • J Chipperfield
  • L Bird

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The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand. / Rodzli, Nazahiyah; Lockhart, Michael; Levy, C W; Chipperfield, J; Bird, L; Baldock, Clair; Prince, Stephen M. .

In: Biophysical Journal, Vol. 119, No. 3, 26.06.2020, p. 667-689.

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Rodzli, Nazahiyah ; Lockhart, Michael ; Levy, C W ; Chipperfield, J ; Bird, L ; Baldock, Clair ; Prince, Stephen M. . / The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand. In: Biophysical Journal. 2020 ; Vol. 119, No. 3. pp. 667-689.

Bibtex

@article{9cdce156da96481fa70211800e21ef6d,
title = "The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand",
abstract = "PSD-95 is a member of Membrane Associated Guanylate Kinase class of proteins which form scaffolding interactions with partner proteins including ion and receptor channels. PSD-95 is directly implicated in modulating the electrical responses of excitable cells. The first two PSD-95/Disks Large/Zona Occludens (PDZ) domains of PSD-95 have been shown to be the key component in the formation of channel clusters. We report crystal structures of this dual domain in both in apo- and ligand-bound form; thermodynamic analysis of ligand association and Small Angle X-ray Scattering of the dual domain in the absence and presence of ligands. These experiments reveal that the ligated double domain forms a 3-dimensional scaffold which can be described by a Spacegroup. The concentration of the components in this study is comparable to those found in compartments of excitable cells such as the postsynaptic density and juxta-paranodes of Ranvier. These in vitro experiments inform the basis of the scaffolding function of PSD-95 and provide a detailed model for scaffold formation by the PDZ domains of PSD-95.",
keywords = "protein-protein interaction, biophysical analysis, clustering, PDZ domain, MAGUK, scaffold protein",
author = "Nazahiyah Rodzli and Michael Lockhart and Levy, {C W} and J Chipperfield and L Bird and Clair Baldock and Prince, {Stephen M.}",
year = "2020",
month = jun,
day = "26",
doi = "10.1016/j.bpj.2020.06.018",
language = "English",
volume = "119",
pages = "667--689",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand

AU - Rodzli, Nazahiyah

AU - Lockhart, Michael

AU - Levy, C W

AU - Chipperfield, J

AU - Bird, L

AU - Baldock, Clair

AU - Prince, Stephen M.

PY - 2020/6/26

Y1 - 2020/6/26

N2 - PSD-95 is a member of Membrane Associated Guanylate Kinase class of proteins which form scaffolding interactions with partner proteins including ion and receptor channels. PSD-95 is directly implicated in modulating the electrical responses of excitable cells. The first two PSD-95/Disks Large/Zona Occludens (PDZ) domains of PSD-95 have been shown to be the key component in the formation of channel clusters. We report crystal structures of this dual domain in both in apo- and ligand-bound form; thermodynamic analysis of ligand association and Small Angle X-ray Scattering of the dual domain in the absence and presence of ligands. These experiments reveal that the ligated double domain forms a 3-dimensional scaffold which can be described by a Spacegroup. The concentration of the components in this study is comparable to those found in compartments of excitable cells such as the postsynaptic density and juxta-paranodes of Ranvier. These in vitro experiments inform the basis of the scaffolding function of PSD-95 and provide a detailed model for scaffold formation by the PDZ domains of PSD-95.

AB - PSD-95 is a member of Membrane Associated Guanylate Kinase class of proteins which form scaffolding interactions with partner proteins including ion and receptor channels. PSD-95 is directly implicated in modulating the electrical responses of excitable cells. The first two PSD-95/Disks Large/Zona Occludens (PDZ) domains of PSD-95 have been shown to be the key component in the formation of channel clusters. We report crystal structures of this dual domain in both in apo- and ligand-bound form; thermodynamic analysis of ligand association and Small Angle X-ray Scattering of the dual domain in the absence and presence of ligands. These experiments reveal that the ligated double domain forms a 3-dimensional scaffold which can be described by a Spacegroup. The concentration of the components in this study is comparable to those found in compartments of excitable cells such as the postsynaptic density and juxta-paranodes of Ranvier. These in vitro experiments inform the basis of the scaffolding function of PSD-95 and provide a detailed model for scaffold formation by the PDZ domains of PSD-95.

KW - protein-protein interaction

KW - biophysical analysis

KW - clustering

KW - PDZ domain

KW - MAGUK

KW - scaffold protein

U2 - 10.1016/j.bpj.2020.06.018

DO - 10.1016/j.bpj.2020.06.018

M3 - Article

VL - 119

SP - 667

EP - 689

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 3

ER -