Using Chemical Genetics and ATP Analogues To Dissect Protein Kinase Function

Protein kinases catalyze the transfer of the γ-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 re...

Full description

Saved in:
Bibliographic Details
Published in:ACS chemical biology 2007-05, Vol.2 (5), p.299-314
Main Authors: Elphick, Lucy M, Lee, Sarah E, Gouverneur, Véronique, Mann, David J
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - analogs & derivatives
Adenosine Triphosphate - chemical synthesis
Animals
Binding Sites
Combinatorial Chemistry Techniques
Humans
Models, Molecular
Phosphorylation
Protein Binding
Protein Engineering
Protein Kinases - chemistry
Protein Kinases - genetics
Protein Kinases - metabolism
Substrate Specificity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Protein kinases catalyze the transfer of the γ-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.
ISSN:1554-8929
1554-8937
DOI:10.1021/cb700027u