TY - JOUR T1 - Inhibition of Protein Kinases by Balanol: Specificity within the Serine/Threonine Protein Kinase Subfamily JF - Molecular Pharmacology JO - Mol Pharmacol SP - 370 LP - 376 DO - 10.1124/mol.56.2.370 VL - 56 IS - 2 AU - Juliana Setyawan AU - Kazunori Koide AU - Thomas C. Diller AU - Mark E. Bunnage AU - Susan S. Taylor AU - K. C. Nicolaou AU - Laurence L. Brunton Y1 - 1999/08/01 UR - http://molpharm.aspetjournals.org/content/56/2/370.abstract N2 - Balanol is a potent inhibitor of cyclic AMP-dependent protein kinase and protein kinase C, acting competitively with ATP with an affinity 3000 times that of ATP. We tested the capacity of balanol to inhibit representative serine- and threonine-specific protein kinases from the protein kinase subfamily that shares a common conserved catalytic core with cyclic AMP-dependent protein kinase. Balanol’s pattern of interactions indicates considerable diversity of the ATP/balanol-binding sites of protein kinases within familial groups and even among isoforms of the same kinase. We propose that balanol is a protean structure that may be modified to produce selective, high-affinity inhibitors and probes of the ATP-binding sites of serine/threonine protein kinases. ER -