Exploiting the promiscuity of imatinib

J Biol. 2009;8(3):30. doi: 10.1186/jbiol134. Epub 2009 Apr 15.

Abstract

The protein kinase inhibitor imatinib, also known as Gleevec, has been a notable success in treating chronic myelogenous leukemia. A recent paper in BMC Structural Biology reports a 1.75 A crystal structure of imatinib bound to the oxidoreductase NQO2 and reveals insights into the binding specificity and the off-target effects of the inhibitor.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Benzamides
  • Fusion Proteins, bcr-abl / antagonists & inhibitors
  • Humans
  • Imatinib Mesylate
  • Leukemia, Myelogenous, Chronic, BCR-ABL Positive / drug therapy
  • Molecular Structure
  • Piperazines / chemistry
  • Piperazines / pharmacokinetics*
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / pharmacokinetics
  • Pyrimidines / chemistry
  • Pyrimidines / pharmacokinetics*
  • Quinone Reductases / antagonists & inhibitors
  • Quinone Reductases / chemistry
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Benzamides
  • Piperazines
  • Protein Kinase Inhibitors
  • Pyrimidines
  • Imatinib Mesylate
  • NRH - quinone oxidoreductase2
  • Quinone Reductases
  • Fusion Proteins, bcr-abl