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PDZ domains and their binding partners: structure, specificity, and modification

PDZ domains are abundant protein interaction modules that often recognize short amino acid motifs at the C-termini of target proteins. They regulate multiple biological processes such as transport, ion channel signaling, and other signal transduction systems. This review discusses the structural cha...

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Detalles Bibliográficos
Autores principales: Lee, Ho-Jin, Zheng, Jie J
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2891790/
https://www.ncbi.nlm.nih.gov/pubmed/20509869
http://dx.doi.org/10.1186/1478-811X-8-8
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author Lee, Ho-Jin
Zheng, Jie J
author_facet Lee, Ho-Jin
Zheng, Jie J
author_sort Lee, Ho-Jin
collection PubMed
description PDZ domains are abundant protein interaction modules that often recognize short amino acid motifs at the C-termini of target proteins. They regulate multiple biological processes such as transport, ion channel signaling, and other signal transduction systems. This review discusses the structural characterization of PDZ domains and the use of recently emerging technologies such as proteomic arrays and peptide libraries to study the binding properties of PDZ-mediated interactions. Regulatory mechanisms responsible for PDZ-mediated interactions, such as phosphorylation in the PDZ ligands or PDZ domains, are also discussed. A better understanding of PDZ protein-protein interaction networks and regulatory mechanisms will improve our knowledge of many cellular and biological processes.
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spelling pubmed-28917902010-06-25 PDZ domains and their binding partners: structure, specificity, and modification Lee, Ho-Jin Zheng, Jie J Cell Commun Signal Review PDZ domains are abundant protein interaction modules that often recognize short amino acid motifs at the C-termini of target proteins. They regulate multiple biological processes such as transport, ion channel signaling, and other signal transduction systems. This review discusses the structural characterization of PDZ domains and the use of recently emerging technologies such as proteomic arrays and peptide libraries to study the binding properties of PDZ-mediated interactions. Regulatory mechanisms responsible for PDZ-mediated interactions, such as phosphorylation in the PDZ ligands or PDZ domains, are also discussed. A better understanding of PDZ protein-protein interaction networks and regulatory mechanisms will improve our knowledge of many cellular and biological processes. BioMed Central 2010-05-28 /pmc/articles/PMC2891790/ /pubmed/20509869 http://dx.doi.org/10.1186/1478-811X-8-8 Text en Copyright ©2010 Lee and Zheng; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Lee, Ho-Jin
Zheng, Jie J
PDZ domains and their binding partners: structure, specificity, and modification
title PDZ domains and their binding partners: structure, specificity, and modification
title_full PDZ domains and their binding partners: structure, specificity, and modification
title_fullStr PDZ domains and their binding partners: structure, specificity, and modification
title_full_unstemmed PDZ domains and their binding partners: structure, specificity, and modification
title_short PDZ domains and their binding partners: structure, specificity, and modification
title_sort pdz domains and their binding partners: structure, specificity, and modification
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2891790/
https://www.ncbi.nlm.nih.gov/pubmed/20509869
http://dx.doi.org/10.1186/1478-811X-8-8
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