Three-Dimensional Structure of ras p21 Proteins
ras genes (review in Barbacid, 1987) have been found in a large number of eukaryotic organisms, from Saccharomyces and Drosophila to chicken, rat, and man. Moreover, ras gene products of various species show a very high degree of homology: even between proteins from yeast and man there is approximately 54% identity between corresponding amino acids, and ras proteins from chicken and man differ only in three amino acids. Such evolutionary conservation implies an important cellular function for these proteins, and they have indeed been implicated in playing a crucial role in cell proliferation and terminal differentiation. Based on these observations and on biochemical similarities with G-proteins, it is thought that ras proteins participate as signal transducers at the beginning of the cascade of reactions leading to various essential cellular processes.
KeywordsGTPase Activity Guanine Base Murine Sarcoma Virus Stanford Synchrotron Radiation Laboratory GTPase Reaction
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- Kim, S.-H., De Vos, A. M., Tong, L., Milburn, M. V., Matias, P. M., Jancarik, J., Ohtsuka, E., and Nishimura, S., 1988, ras oncogene proteins: three-dimensional structures, functional implications, and a model for signal transduction, Cold Spring Harbor Symp., in press.Google Scholar
- Miura, K., Inoue, Y., Nakamori, H., Iwai, S., Ohtsuka, E., Ikehora, M., Noguchi, S., and Nishimura, S., 1986, Synthesis and expression of a synthetic gene for the activated human c-Ha-ras protein, Jpn. J. Canc. Res. (Gann), 77:45.Google Scholar
- Shih, T. Y., Stokes, P. E., Smythers, G. W., Dhar, D., and Oroszlan, S., 1982, Characterization of the phosphorylation sites and the surrounding amino acid sequences of the p21 transforming proteins coded for by the Harvey and Kirsten strains of murine sarcoma viruses, J. Biol. Chem., 257:11767.PubMedGoogle Scholar
- Tronrud, D. E., Ten Eyck, L. F., and Matthews, B. W., 1987, An efficient general-purpose least-squares program for macromolecular structures, Acta Cryst., A43:489.Google Scholar
- Webb, M. R. and Eccleston, J. F., 1981, The stereochemical course of the ribosome-dependent GTPase reaction of elongation factor G from Escherichia coli, J. Biol. Chem., 256:7734.Google Scholar