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Towards the computational design of protein post-translational regulation
Protein post-translational modifications (PTMs) are a fast and versatility mechanism used by the cell to regulate the function of proteins in response to changing conditions. PTMs can alter the activity of proteins by allosteric regulation or by controlling protein interactions, localization and abu...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4673319/ https://www.ncbi.nlm.nih.gov/pubmed/25956846 http://dx.doi.org/10.1016/j.bmc.2015.04.056 |
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author | Strumillo, Marta Beltrao, Pedro |
author_facet | Strumillo, Marta Beltrao, Pedro |
author_sort | Strumillo, Marta |
collection | PubMed |
description | Protein post-translational modifications (PTMs) are a fast and versatility mechanism used by the cell to regulate the function of proteins in response to changing conditions. PTMs can alter the activity of proteins by allosteric regulation or by controlling protein interactions, localization and abundance. Recent advances in proteomics have revealed the extent of regulation by PTMs and the different mechanisms used in nature to exert control over protein function via PTMs. These developments can serve as the foundation for the rational design of protein regulation. Here we review the advances in methods to determine the function of PTMs, protein allosteric control and examples of rational design of PTM regulation. These advances create an opportunity to move synthetic biology forward by making use of a level of regulation that is of yet unexplored. |
format | Online Article Text |
id | pubmed-4673319 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-46733192015-12-29 Towards the computational design of protein post-translational regulation Strumillo, Marta Beltrao, Pedro Bioorg Med Chem Article Protein post-translational modifications (PTMs) are a fast and versatility mechanism used by the cell to regulate the function of proteins in response to changing conditions. PTMs can alter the activity of proteins by allosteric regulation or by controlling protein interactions, localization and abundance. Recent advances in proteomics have revealed the extent of regulation by PTMs and the different mechanisms used in nature to exert control over protein function via PTMs. These developments can serve as the foundation for the rational design of protein regulation. Here we review the advances in methods to determine the function of PTMs, protein allosteric control and examples of rational design of PTM regulation. These advances create an opportunity to move synthetic biology forward by making use of a level of regulation that is of yet unexplored. Elsevier Science 2015-06-15 /pmc/articles/PMC4673319/ /pubmed/25956846 http://dx.doi.org/10.1016/j.bmc.2015.04.056 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Strumillo, Marta Beltrao, Pedro Towards the computational design of protein post-translational regulation |
title | Towards the computational design of protein post-translational regulation |
title_full | Towards the computational design of protein post-translational regulation |
title_fullStr | Towards the computational design of protein post-translational regulation |
title_full_unstemmed | Towards the computational design of protein post-translational regulation |
title_short | Towards the computational design of protein post-translational regulation |
title_sort | towards the computational design of protein post-translational regulation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4673319/ https://www.ncbi.nlm.nih.gov/pubmed/25956846 http://dx.doi.org/10.1016/j.bmc.2015.04.056 |
work_keys_str_mv | AT strumillomarta towardsthecomputationaldesignofproteinposttranslationalregulation AT beltraopedro towardsthecomputationaldesignofproteinposttranslationalregulation |