p21 with a phenylalanine 28----leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties.

Abstract

The H-ras gene product p21H has been mutated at Phe-28, which makes a hydrophobic interaction with the guanine base of bound GDP/GTP. The mutation Phe-28----Leu drastically increases nucleotide dissociation rates without affecting association rates. This is due to a perturbed binding of base, alpha- and beta-phosphate, and Mg2+, as evidenced from 31P NMR… (More)

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@article{Reinstein1991p21WA, title={p21 with a phenylalanine 28----leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties.}, author={Jochen Reinstein and Ilme Schlichting and Marianne Frech and Roger S. Goody and Alfred Wittinghofer}, journal={The Journal of biological chemistry}, year={1991}, volume={266 26}, pages={17700-6} }