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- W2045261036 endingPage "3477" @default.
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- W2045261036 abstract "The function of Gly-60, the conserved glycine in the DXXG domain of v-H-ras, was examined by site-directed mutagenesis. It was found that while the G60A (Gly-60 to Ala substitution) mutation has little effect on the interaction of H-ras with guanine nucleotides, it completely abolishes the biological activity of v-H-ras. The G60A mutation also exerts little effect on the interaction of H-ras with SDC25C (a guanine nucleotide exchange factor) and GAP. However, the G60A mutation does lower the ability of H-ras to bind Raf. GTP induces an enhancement of fluorescence emission in complexes consisting of H-ras and the fluorescent dye 8-anilino-1-naphthalenesulfonic acid. This enhancement is blocked by the G60A mutation. On the basis of these observations, we propose that the GTP-induced conformational change of H-ras, a process required for H-ras activities, is impaired by the G60A mutation." @default.
- W2045261036 created "2016-06-24" @default.
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- W2045261036 date "1995-03-01" @default.
- W2045261036 modified "2023-09-23" @default.
- W2045261036 title "Mutagenesis of the H-ras p21 at glycine-60 residue disrupts GTP-induced conformational change" @default.
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- W2045261036 doi "https://doi.org/10.1021/bi00010a040" @default.
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