Walter M, Clark S G, Levinson A D
Science. 1986 Aug 8;233(4764):649-52. doi: 10.1126/science.3487832.
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.
在基于结构原因被认为是与鸟嘌呤核苷酸接触位点的位置（第116位残基），将单个氨基酸变化引入人H-ras蛋白的正常（非致癌）和活化形式中。该位点的取代可显著降低两种形式结合和水解鸟苷5'-三磷酸的能力；然而，这些取代不一定会削弱活化衍生物的转化能力。一种严重损害这些功能的取代激活了原本正常多肽的转化潜力。
