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Science 8 August 1986:
Vol. 233. no. 4764, pp. 649 - 652
DOI: 10.1126/science.3487832
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Articles

Science, Vol 233, Issue 4764, 649-652
Copyright © 1986 by American Association for the Advancement of Science

articles

The oncogenic activation of human p21ras by a novel mechanism

M Walter, SG Clark, and AD Levinson

Single amino acid changes were introduced into normal (non-oncogenic) and activated forms of the human H-ras protein at a position (residue 116) proposed on structural grounds to represent a contact site with guanine nucleotides. Substitutions at this site could significantly reduce the ability of both forms to bind and hydrolyze guanosine 5'-triphosphate; these substitutions, however, did not necessarily diminish the transforming capacity of activated derivatives. One substitution that severely impairs these functions activated the transforming potential of the otherwise normal polypeptide.


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