Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras

Nat Struct Biol. 1997 Sep;4(9):686-9. doi: 10.1038/nsb0997-686.

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.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arginine / chemistry*
  • Binding Sites
  • GTP Phosphohydrolases / chemistry*
  • GTPase-Activating Proteins
  • Guanosine Triphosphate / metabolism
  • Proteins / chemistry*
  • ras GTPase-Activating Proteins
  • ras Proteins / chemistry*

Substances

  • GTPase-Activating Proteins
  • Proteins
  • ras GTPase-Activating Proteins
  • Guanosine Triphosphate
  • Arginine
  • GTP Phosphohydrolases
  • ras Proteins