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

Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Structural & Molecular Biology Springer Journals

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

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References (43)

Publisher
Springer Journals
Copyright
Copyright © 1997 by Nature Publishing Group
Subject
Life Sciences; Life Sciences, general; Biochemistry, general; Protein Structure; Membrane Biology; Biological Microscopy
ISSN
1545-9993
eISSN
1545-9985
DOI
10.1038/nsb0997-686
Publisher site
See Article on Publisher Site

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 RasṁRasGAP complex.

Journal

Nature Structural & Molecular BiologySpringer Journals

Published: Sep 1, 1997

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