The oncogenic activation of human p21ras by a novel mechanism.
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.
D000595:Amino Acid Sequence; D002471:Cell Transformation, Neoplastic / Q000378:metabolism; D004247:DNA / Q000235:genetics; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D009363:Neoplasm Proteins / Q000235:genetics* / Q000378:metabolism; D015689:Oncogene Protein p21(ras); D009857:Oncogenes
D009363:Neoplasm Proteins; D006160:Guanosine Triphosphate; D004247:DNA; D015689:Oncogene Protein p21(ras)