Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors.

@article{Xu1996StructuralBF,
  title={Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors.},
  author={Richard Xu and Gilles Carmel and Jeff Kuret and Xiaodong Cheng},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1996},
  volume={93 13},
  pages={6308-13}
}
A large family of isoquinoline sulfonamide compounds inhibits protein kinases by competing with adenosine triphosphates(ATP), yet interferes little with the activity of other ATP-using enzymes such as ATPases and adenylate cyclases. One such compound, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide (CK17), is selective for casein kinase-1 isolated from… CONTINUE READING