Ligand binding by PDZ domains

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Ligand binding by PDZ domains. / Chi, Celestine N.; Bach, Anders; Strømgaard, Kristian; Gianni, Stefano; Jemth, Per.

In: BioFactors, Vol. 38, No. 5, 2012, p. 338-348 (Review).

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Chi, CN, Bach, A, Strømgaard, K, Gianni, S & Jemth, P 2012, 'Ligand binding by PDZ domains', BioFactors, vol. 38, no. 5, pp. 338-348 (Review). https://doi.org/10.1002/biof.1031

APA

Chi, C. N., Bach, A., Strømgaard, K., Gianni, S., & Jemth, P. (2012). Ligand binding by PDZ domains. BioFactors, 38(5), 338-348 (Review). https://doi.org/10.1002/biof.1031

Vancouver

Chi CN, Bach A, Strømgaard K, Gianni S, Jemth P. Ligand binding by PDZ domains. BioFactors. 2012;38(5):338-348 (Review). https://doi.org/10.1002/biof.1031

Author

Chi, Celestine N. ; Bach, Anders ; Strømgaard, Kristian ; Gianni, Stefano ; Jemth, Per. / Ligand binding by PDZ domains. In: BioFactors. 2012 ; Vol. 38, No. 5. pp. 338-348 (Review).

Bibtex

@article{5373ffc5ff1a4de99ee4f987b79036e1,
title = "Ligand binding by PDZ domains",
abstract = "The postsynaptic density protein-95/disks large/zonula occludens-1 (PDZ) protein domain family is one of the most common protein-protein interaction modules in mammalian cells, with paralogs present in several hundred human proteins. PDZ domains are found in most cell types, but neuronal proteins, for example, are particularly rich in these domains. The general function of PDZ domains is to bring proteins together within the appropriate cellular compartment, thereby facilitating scaffolding, signaling, and trafficking events. The many functions of PDZ domains under normal physiological as well as pathological conditions have been reviewed recently. In this review, we focus on the molecular details of how PDZ domains bind their protein ligands and their potential as drug targets in this context.",
keywords = "Animals, Binding Sites, Humans, Ligands, Models, Molecular, Nerve Tissue Proteins, Nervous System Diseases, PDZ Domains, Peptidomimetics, Protein Binding, Protein Structure, Secondary, Protein Transport, Signal Transduction",
author = "Chi, {Celestine N.} and Anders Bach and Kristian Str{\o}mgaard and Stefano Gianni and Per Jemth",
note = "Copyright {\textcopyright} 2012 International Union of Biochemistry and Molecular Biology, Inc.",
year = "2012",
doi = "10.1002/biof.1031",
language = "English",
volume = "38",
pages = "338--348 (Review)",
journal = "BioFactors",
issn = "0951-6433",
publisher = "Wiley",
number = "5",

}

RIS

TY - JOUR

T1 - Ligand binding by PDZ domains

AU - Chi, Celestine N.

AU - Bach, Anders

AU - Strømgaard, Kristian

AU - Gianni, Stefano

AU - Jemth, Per

N1 - Copyright © 2012 International Union of Biochemistry and Molecular Biology, Inc.

PY - 2012

Y1 - 2012

N2 - The postsynaptic density protein-95/disks large/zonula occludens-1 (PDZ) protein domain family is one of the most common protein-protein interaction modules in mammalian cells, with paralogs present in several hundred human proteins. PDZ domains are found in most cell types, but neuronal proteins, for example, are particularly rich in these domains. The general function of PDZ domains is to bring proteins together within the appropriate cellular compartment, thereby facilitating scaffolding, signaling, and trafficking events. The many functions of PDZ domains under normal physiological as well as pathological conditions have been reviewed recently. In this review, we focus on the molecular details of how PDZ domains bind their protein ligands and their potential as drug targets in this context.

AB - The postsynaptic density protein-95/disks large/zonula occludens-1 (PDZ) protein domain family is one of the most common protein-protein interaction modules in mammalian cells, with paralogs present in several hundred human proteins. PDZ domains are found in most cell types, but neuronal proteins, for example, are particularly rich in these domains. The general function of PDZ domains is to bring proteins together within the appropriate cellular compartment, thereby facilitating scaffolding, signaling, and trafficking events. The many functions of PDZ domains under normal physiological as well as pathological conditions have been reviewed recently. In this review, we focus on the molecular details of how PDZ domains bind their protein ligands and their potential as drug targets in this context.

KW - Animals

KW - Binding Sites

KW - Humans

KW - Ligands

KW - Models, Molecular

KW - Nerve Tissue Proteins

KW - Nervous System Diseases

KW - PDZ Domains

KW - Peptidomimetics

KW - Protein Binding

KW - Protein Structure, Secondary

KW - Protein Transport

KW - Signal Transduction

U2 - 10.1002/biof.1031

DO - 10.1002/biof.1031

M3 - Journal article

C2 - 22674855

VL - 38

SP - 338-348 (Review)

JO - BioFactors

JF - BioFactors

SN - 0951-6433

IS - 5

ER -

ID: 45807203