Article
X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.
Proceedings of the National Academy of Sciences of the United States of America - 15 Apr 1992
Privé G G, Milburn M V, Tong L, de Vos A M, Yamaizumi Z, Nishimura S, Kim S H
Abstract excerpt
RAS genes isolated from human tumors often have mutations at positions corresponding to amino acid 12 or 61 of the encoded protein (p21), while retroviral ras-encoded p21 contains substitutions at both positions 12 and 59. These mutant proteins are deficient in their GTP hydrolysis activity, and this loss of activity is linked to their transforming potential. The crystal structures of the mutant proteins are...
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