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Exploiting the promiscuity of imatinib

Shun J Lee12 and Jean YJ Wang123*

Author Affiliations

1 Department of Medicine and Division of Hematology-Oncology, 3855 Health Sciences Drive, University of California, San Diego, La Jolla, CA 92093, USA

2 Moores Cancer Center, 3855 Health Sciences Drive, University of California, San Diego, La Jolla, CA 92093, USA

3 Division of Biological Sciences, 3855 Health Sciences Drive, University of California, San Diego, La Jolla, CA 92093, USA

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Journal of Biology 2009, 8:30  doi:10.1186/jbiol134

Published: 15 April 2009

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 Å crystal structure of imatinib bound to the oxidoreductase NQO2 and reveals insights into the binding specificity and the off-target effects of the inhibitor.