Using chemical genetics and ATP analogues to dissect protein kinase function

被引:52
作者
Elphick, Lucy M.
Lee, Sarah E.
Gouverneur, Veronique
Mann, David J. [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Cell Cycle Lab, Div Cell & Mol Biol, London SW7 2AZ, England
[2] Univ Oxford, Chem Res Lab, Oxford OX1 3TA, England
基金
英国生物技术与生命科学研究理事会;
关键词
D O I
10.1021/cb700027u
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 kinases catalyze the transfer of the -phosphate of ATP to a protein substrate and thereby profoundly alter the properties of the phosphorylated protein. The identification of the substrates of protein kinases has proven to be a very difficult task because of the multitude of structurally related protein kinases present in cells, their apparent redundancy of function, and the lack of absolute specificity of small-molecule inhibitors. Here, we review approaches that utilize chemical genetics to determine the functions and substrates of protein kinases, focusing on the design of ATP analogues and protein kinase binding site mutants.
引用
收藏
页码:299 / 314
页数:16
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