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Chronic myeloid leukemia is attributed to the BCR-Abl fusion protein's kinase enzyme activity. We present the 2. 4-square model of bosutinib bound to Abl's kinase domain, which explains the inhibitor's ability against several imatinib-resistant mutants, as well as the fact that similar inhibitors lacking a nitrile moiety might be highly effective against the common T315I mutant. We demonstrate that the fluorescence characteristics of these compounds enable inhibition binding to be measured quantitatively, and that the infrared absorption of the nitrile group reveals a different electrostatic environment in the conserved ATP-binding sites of Abl and Src kinases.
Source link: https://doi.org/10.1371/journal.pone.0029828
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