Unit

UNIT 2.9 The Human Kinome and Kinase Inhibition

  1. Krisna C. Duong-Ly,
  2. Jeffrey R. Peterson

Published Online: 1 MAR 2013

DOI: 10.1002/0471141755.ph0209s60

Current Protocols in Pharmacology

Current Protocols in Pharmacology

How to Cite

Duong-Ly, K. C. and Peterson, J. R. 2013. The Human Kinome and Kinase Inhibition. Current Protocols in Pharmacology. 60:2.9:2.9.1–2.9.14.

Author Information

  1. Cancer Biology Program, Fox Chase Cancer Center, Philadelphia, Pennsylvania

Publication History

  1. Published Online: 1 MAR 2013

Abstract

Protein and lipid kinases play key regulatory roles in a number of biological processes. Unsurprisingly, activating mutations in kinases have been linked to a number of disorders and diseases, most notably cancers. Thus, kinases have emerged as promising clinical targets. There are more than 500 human protein kinases and about 20 lipid kinases. Most protein kinases share a highly conserved domain, the eukaryotic protein kinase (ePK) domain, which contains the ATP and substrate-binding sites. Many inhibitors in clinical use bind to the highly conserved ATP binding site. For this reason, many kinase inhibitors are not exclusively selective for their intended targets. Furthermore, despite the current interest in kinase inhibitors, very few kinases implicated in disease have validated inhibitors. This unit describes the human kinome, ePK structure, and types of kinase inhibitors, focusing on methods to identify potent and selective kinase inhibitors. Curr. Protoc. Pharmacol. 60:2.9.1-2.9.14. © 2013 by John Wiley & Sons, Inc.

Keywords:

  • kinase;
  • small-molecule inhibition;
  • inhibitor selectivity;
  • inhibitor screening;
  • kinase domain;
  • kinase assay