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

Nature Structural Biology volume 4, pages 686–689 (1997)Cite this article

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 RasṁRasGAP complex.

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Authors and Affiliations

  1. Max-Planck-Institut für molekulare Physiologie, Rheinlanddamm 201, 44139, Dortmund, Germany

    Mohammad Reza Ahmadian, Patricia Stege, Klaus Scheffzek & Alfred Wittinghofer

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  1. Mohammad Reza Ahmadian
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  2. Patricia Stege
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  3. Klaus Scheffzek
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  4. Alfred Wittinghofer
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Ahmadian, M., Stege, P., Scheffzek, K. et al. Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nat Struct Mol Biol 4, 686–689 (1997). https://doi.org/10.1038/nsb0997-686

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