title: Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras.
abstract: RasGAPs supply a catalytic residue, termed the arginine finger,into the active site of Ras thereby stabilizing the transition state of the GTPase reaction and increasing the reaction rate by more than one thousand-fold, in good agreement with the structure of the Ras.RasGAP complex.
authors.forename: M R
authors.initials: MR
authors.lastname: Ahmadian
authors.forename: P
authors.initials: P
authors.lastname: Stege
authors.forename: K
authors.initials: K
authors.lastname: Scheffzek
authors.forename: A
authors.initials: A
authors.lastname: Wittinghofer
mesh_terms: D001120:Arginine / Q000737:chemistry*; D001665:Binding Sites; D020558:GTP Phosphohydrolases / Q000737:chemistry*; D020690:GTPase-Activating Proteins; D006160:Guanosine Triphosphate / Q000378:metabolism; D011506:Proteins / Q000737:chemistry*; D020703:ras GTPase-Activating Proteins; D018631:ras Proteins / Q000737:chemistry*
chemical_list: D020690:GTPase-Activating Proteins; D011506:Proteins; D020703:ras GTPase-Activating Proteins; D006160:Guanosine Triphosphate; D001120:Arginine; D020558:GTP Phosphohydrolases; D018631:ras Proteins