title: Towards the computational design of protein post-translational regulation.
abstract: 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.
authors.affiliation: European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge CB10 1SD, UK.
authors.forename: Marta
authors.initials: M
authors.lastname: Strumillo
authors.affiliation: European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge CB10 1SD, UK; iBiMED and Department of Health Sciences, University of Aveiro, 3810-193 Aveiro, Portugal. Electronic address: pbeltrao@ebi.ac.uk.
authors.forename: Pedro
authors.initials: P
authors.lastname: Beltrao
mesh_terms: D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D060066:Protein Interaction Maps; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000032:analysis / Q000378:metabolism*; D059748:Proteolysis
chemical_list: D011506:Proteins
keywords: Allosteric; Bioinformatics; PTMs