Towards the computational design of protein post-translational regulation

被引：21
作者：
Strumillo, Marta [1 ]
Beltrao, Pedro [1 ,2 ,3 ]
机构：
[1] European Bioinformat Inst, European Mol Biol Lab, Cambridge CB10 1SD, England
[2] Univ Aveiro, iBiMED, P-3810193 Aveiro, Portugal
[3] Univ Aveiro, Dept Hlth Sci, P-3810193 Aveiro, Portugal
来源：
BIOORGANIC & MEDICINAL CHEMISTRY | 2015年 / 23卷 / 12期
关键词：
Bioinformatics; PTMs; Allosteric; KINASE-INDUCIBLE DOMAIN; SMOOTH-MUSCLE MYOSIN; LIVING CELLS; CONFORMATIONAL-CHANGES; ALLOSTERIC MECHANISM; MOLECULAR-DYNAMICS; LYSINE ACETYLATION; CROSS-TALK; PHOSPHORYLATION; ACTIVATION;
D O I：
10.1016/j.bmc.2015.04.056
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2015 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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收藏
页码：2877 / 2882
页数：6
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