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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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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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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. |
format | Text |
id | pubmed-2891790 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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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