Ligand binding to the PDZ domains of postsynaptic density protein 95

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Ligand binding to the PDZ domains of postsynaptic density protein 95. / Toto, Angelo; Pedersen, Søren W; Karlsson, O Andreas; Moran, Griffin E; Andersson, Eva; Chi, Celestine N; Strømgaard, Kristian; Gianni, Stefano; Jemth, Per.

In: Protein Engineering Design and Selection (Print), Vol. 29, No. 5, 05.2016, p. 169-75.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Toto, A, Pedersen, SW, Karlsson, OA, Moran, GE, Andersson, E, Chi, CN, Strømgaard, K, Gianni, S & Jemth, P 2016, 'Ligand binding to the PDZ domains of postsynaptic density protein 95', Protein Engineering Design and Selection (Print), vol. 29, no. 5, pp. 169-75. https://doi.org/10.1093/protein/gzw004

APA

Toto, A., Pedersen, S. W., Karlsson, O. A., Moran, G. E., Andersson, E., Chi, C. N., Strømgaard, K., Gianni, S., & Jemth, P. (2016). Ligand binding to the PDZ domains of postsynaptic density protein 95. Protein Engineering Design and Selection (Print), 29(5), 169-75. https://doi.org/10.1093/protein/gzw004

Vancouver

Toto A, Pedersen SW, Karlsson OA, Moran GE, Andersson E, Chi CN et al. Ligand binding to the PDZ domains of postsynaptic density protein 95. Protein Engineering Design and Selection (Print). 2016 May;29(5):169-75. https://doi.org/10.1093/protein/gzw004

Author

Toto, Angelo ; Pedersen, Søren W ; Karlsson, O Andreas ; Moran, Griffin E ; Andersson, Eva ; Chi, Celestine N ; Strømgaard, Kristian ; Gianni, Stefano ; Jemth, Per. / Ligand binding to the PDZ domains of postsynaptic density protein 95. In: Protein Engineering Design and Selection (Print). 2016 ; Vol. 29, No. 5. pp. 169-75.

Bibtex

@article{df6cb43d1aeb46189ac7aadb5ba39de6,
title = "Ligand binding to the PDZ domains of postsynaptic density protein 95",
abstract = "Cellular scaffolding and signalling is generally governed by multidomain proteins, where each domain has a particular function. Postsynaptic density protein 95 (PSD-95) is involved in synapse formation and is a typical example of such a multidomain protein. Protein-protein interactions of PSD-95 are well studied and include the following three protein ligands: (i)N-methyl-d-aspartate-type ionotropic glutamate receptor subunit GluN2B, (ii) neuronal nitric oxide synthase and (iii) cysteine-rich protein (CRIPT), all of which bind to one or more of the three PDZ domains in PSD-95. While interactions for individual PDZ domains of PSD-95 have been well studied, less is known about the influence of neighbouring domains on the function of the respective individual domain. We therefore performed a systematic study on the ligand-binding kinetics of PSD-95 using constructs of different size for PSD-95 and its ligands. Regarding the canonical peptide-binding pocket and relatively short peptides (up to 15-mer), the PDZ domains in PSD-95 by and large work as individual binding modules. However, in agreement with previous studies, residues outside of the canonical binding pocket modulate the affinity of the ligands. In particular, the dissociation of the 101 amino acid CRIPT from PSD-95 is slowed down at least 10-fold for full-length PSD-95 when compared with the individual PDZ3 domain.",
keywords = "Journal Article, Research Support, Non-U.S. Gov't",
author = "Angelo Toto and Pedersen, {S{\o}ren W} and Karlsson, {O Andreas} and Moran, {Griffin E} and Eva Andersson and Chi, {Celestine N} and Kristian Str{\o}mgaard and Stefano Gianni and Per Jemth",
note = "{\textcopyright} The Author 2016. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.",
year = "2016",
month = may,
doi = "10.1093/protein/gzw004",
language = "English",
volume = "29",
pages = "169--75",
journal = "Protein Engineering, Design and Selection",
issn = "1741-0126",
publisher = "Oxford University Press",
number = "5",

}

RIS

TY - JOUR

T1 - Ligand binding to the PDZ domains of postsynaptic density protein 95

AU - Toto, Angelo

AU - Pedersen, Søren W

AU - Karlsson, O Andreas

AU - Moran, Griffin E

AU - Andersson, Eva

AU - Chi, Celestine N

AU - Strømgaard, Kristian

AU - Gianni, Stefano

AU - Jemth, Per

N1 - © The Author 2016. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.

PY - 2016/5

Y1 - 2016/5

N2 - Cellular scaffolding and signalling is generally governed by multidomain proteins, where each domain has a particular function. Postsynaptic density protein 95 (PSD-95) is involved in synapse formation and is a typical example of such a multidomain protein. Protein-protein interactions of PSD-95 are well studied and include the following three protein ligands: (i)N-methyl-d-aspartate-type ionotropic glutamate receptor subunit GluN2B, (ii) neuronal nitric oxide synthase and (iii) cysteine-rich protein (CRIPT), all of which bind to one or more of the three PDZ domains in PSD-95. While interactions for individual PDZ domains of PSD-95 have been well studied, less is known about the influence of neighbouring domains on the function of the respective individual domain. We therefore performed a systematic study on the ligand-binding kinetics of PSD-95 using constructs of different size for PSD-95 and its ligands. Regarding the canonical peptide-binding pocket and relatively short peptides (up to 15-mer), the PDZ domains in PSD-95 by and large work as individual binding modules. However, in agreement with previous studies, residues outside of the canonical binding pocket modulate the affinity of the ligands. In particular, the dissociation of the 101 amino acid CRIPT from PSD-95 is slowed down at least 10-fold for full-length PSD-95 when compared with the individual PDZ3 domain.

AB - Cellular scaffolding and signalling is generally governed by multidomain proteins, where each domain has a particular function. Postsynaptic density protein 95 (PSD-95) is involved in synapse formation and is a typical example of such a multidomain protein. Protein-protein interactions of PSD-95 are well studied and include the following three protein ligands: (i)N-methyl-d-aspartate-type ionotropic glutamate receptor subunit GluN2B, (ii) neuronal nitric oxide synthase and (iii) cysteine-rich protein (CRIPT), all of which bind to one or more of the three PDZ domains in PSD-95. While interactions for individual PDZ domains of PSD-95 have been well studied, less is known about the influence of neighbouring domains on the function of the respective individual domain. We therefore performed a systematic study on the ligand-binding kinetics of PSD-95 using constructs of different size for PSD-95 and its ligands. Regarding the canonical peptide-binding pocket and relatively short peptides (up to 15-mer), the PDZ domains in PSD-95 by and large work as individual binding modules. However, in agreement with previous studies, residues outside of the canonical binding pocket modulate the affinity of the ligands. In particular, the dissociation of the 101 amino acid CRIPT from PSD-95 is slowed down at least 10-fold for full-length PSD-95 when compared with the individual PDZ3 domain.

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1093/protein/gzw004

DO - 10.1093/protein/gzw004

M3 - Journal article

C2 - 26941280

VL - 29

SP - 169

EP - 175

JO - Protein Engineering, Design and Selection

JF - Protein Engineering, Design and Selection

SN - 1741-0126

IS - 5

ER -

ID: 169438280