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Curr Opin Chem Biol. 2008 Feb;12(1):4-10. doi: 10.1016/j.cbpa.2008.01.018. Epub 2008 Mar 7.

Understanding and exploiting substrate recognition by protein kinases.

Author information

1
Department of Pharmacology, Yale University School of Medicine, P.O. Box 208066, 333 Cedar Street, New Haven, CT 06520, United States. ben.turk@yale.edu

Abstract

Protein kinases play a virtually universal role in cellular regulation and are emerging as an important class of new drug targets, yet the cellular functions of most human kinases largely remain obscure. Aspects of substrate recognition common to all kinases in the ATP nucleotide binding site have been exploited in the generation of analog-specific mutants for exploring kinase function and discovering novel protein substrates. Likewise, understanding interactions with the protein substrate, which differ substantially between kinases, can also help to identify substrates and to produce tools for studying kinase pathways, including fluorescent biosensors. Principles of kinase substrate recognition are particularly valuable in guiding bioinformatics and phosphoproteomics approaches that impact our understanding of signaling pathways and networks on a global scale.

PMID:
18282484
PMCID:
PMC2366800
DOI:
10.1016/j.cbpa.2008.01.018
[Indexed for MEDLINE]
Free PMC Article

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