title: Identification of allosteric inhibitors of p21-activated kinase.
abstract: Protein kinases are among the most important drug targets; however the structural conservation of the ATP-binding pocket of kinases can lead to promiscuous inhibition of additional unintended kinase targets. Allosteric inhibitors that target less conserved regions of protein kinases represent an alternative approach that may provide more selective kinase inhibition. In this report, protocols are provided for the screening and identification of Pak1 inhibitors acting via an allosteric mechanism.
authors.affiliation: Cancer Biology Program, Fox Chase Cancer Center, Philadelphia, PA, USA.
authors.forename: Julien
authors.initials: J
authors.lastname: Viaud
authors.forename: Jeffrey R
authors.initials: JR
authors.lastname: Peterson
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D015195:Drug Design; D019204:GTP-Binding Proteins / Q000378:metabolism; D047428:Protein Kinase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D061987:Sf9 Cells; D054462:p21-Activated Kinases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D020741:rho GTP-Binding Proteins
chemical_list: D047428:Protein Kinase Inhibitors; D017346:Protein Serine-Threonine Kinases; D054462:p21-Activated Kinases; D019204:GTP-Binding Proteins; D020741:rho GTP-Binding Proteins