Ligand binding by PDZ domains

Celestine N. Chi; Anders Bach; Kristian Strømgaard; Stefano Gianni; Per Jemth

doi:10.1002/biof.1031

Ligand binding by PDZ domains

Celestine N. Chi, Anders Bach, Kristian Strømgaard, Stefano Gianni, Per Jemth

46 Citations (Scopus)

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.

Original language	English
Journal	BioFactors
Volume	38
Issue number	5
Pages (from-to)	338-348 (Review)
Number of pages	11
ISSN	0951-6433
DOIs	https://doi.org/10.1002/biof.1031
Publication status	Published - Sept 2012

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

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10.1002/biof.1031

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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.",

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year = "2012",

month = sep,

doi = "10.1002/biof.1031",

language = "English",

volume = "38",

pages = "338--348 (Review)",

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TY - JOUR

T1 - Ligand binding by PDZ domains

AU - Chi, Celestine N.

AU - Bach, Anders

AU - Strømgaard, Kristian

AU - Gianni, Stefano

AU - Jemth, Per

PY - 2012/9

Y1 - 2012/9

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

SN - 0951-6433

VL - 38

SP - 338-348 (Review)

JO - BioFactors

JF - BioFactors

IS - 5

ER -

Ligand binding by PDZ domains

Abstract

Keywords

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