Understanding kinase selectivity through energetic analysis of binding site waters.

@article{Robinson2010UnderstandingKS,
  title={Understanding kinase selectivity through energetic analysis of binding site waters.},
  author={Daniel D. Robinson and Woody Sherman and Ramy Farid},
  journal={ChemMedChem},
  year={2010},
  volume={5 4},
  pages={618-27}
}
Kinases remain an important drug target class within the pharmaceutical industry; however, the rational design of kinase inhibitors is plagued by the complexity of gaining selectivity for a small number of proteins within a family of more than 500 related enzymes. Herein we show how a computational method for identifying the location and thermodynamic properties of water molecules within a protein binding site can yield insight into previously inexplicable selectivity and structure-activity… CONTINUE READING