Exploiting the promiscuity of imatinib.
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.
Department of Medicine and Division of Hematology-Oncology, 3855 Health Sciences Drive, University of California-San Diego, La Jolla, CA 92093, USA.
Shun J
SJ
Lee
Jean Y J
JY
Wang
D000818:Animals; D001549:Benzamides; D016044:Fusion Proteins, bcr-abl / Q000037:antagonists & inhibitors; D006801:Humans; D000068877:Imatinib Mesylate; D015464:Leukemia, Myelogenous, Chronic, BCR-ABL Positive / Q000188:drug therapy; D015394:Molecular Structure; D010879:Piperazines / Q000737:chemistry / Q000493:pharmacokinetics*; D047428:Protein Kinase Inhibitors / Q000737:chemistry / Q000493:pharmacokinetics; D011743:Pyrimidines / Q000737:chemistry / Q000493:pharmacokinetics*; D011808:Quinone Reductases / Q000037:antagonists & inhibitors / Q000737:chemistry; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D001549:Benzamides; D010879:Piperazines; D047428:Protein Kinase Inhibitors; D011743:Pyrimidines; D000068877:Imatinib Mesylate; C419642:NRH - quinone oxidoreductase2; D011808:Quinone Reductases; D016044:Fusion Proteins, bcr-abl