Allosteric Interactions between the Myristate- and ATP-Site of the Abl Kinase

@inproceedings{Iacob2011AllostericIB,
  title={Allosteric Interactions between the Myristate- and ATP-Site of the Abl Kinase},
  author={Roxana E. Iacob and Jianming Zhang and Nathanael S Gray and John R. Engen},
  booktitle={PloS one},
  year={2011}
}
Abl kinase inhibitors targeting the ATP binding pocket are currently employed as potent anti-leukemogenic agents but drug resistance has become a significant clinical limitation. Recently, a compound that binds to the myristate pocket of Abl (GNF-5) was shown to act cooperatively with nilotinib, an ATP-competitive inhibitor to target the recalcitrant "T315I" gatekeeper mutant of Bcr-Abl. To uncover an explanation for how drug binding at a distance from the kinase active site could lead to… CONTINUE READING