Leukemia
Conformation-specific binding involved in cancer drug resistance
Published in Cancer Weekly, May 17th, 2005
"Structural studies suggest that most point mutations in the BCR-ABL kinase domain cause resistance to the ABL kinase inhibitor imatinib by impairing the flexibility of the kinase domain, restricting its ability to adopt the inactive conformation required for optimal imatinib binding, rather than by directly interfering with drug contact residues," scientists reported in the journal Proceedings of the National Academy of Sciences USA.
"BMS-354825, currently in clinical development for imatinib-resistant chronic myelogenous leukemia, is a dual SRC/ABL kinase...
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Source: Cancer Weekly (2005-05-17)
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