Abstract
The 3-dimensional crystal structure of oncomodulin from X-ray analysis reveals that it is quite similar to that of parvalbumin (F. Ahmed et al., in preparation). Oncomodulin has three domains composed of helix:metal-binding loop:helix arranged in a similar way to parvalbumin (Moews and Kretsinger 1975). This was not unexpected because it was known that oncomodulin and parvalbumin share 50% identical amino acid sequence, and an additional 30% conservative residue replacement (MacManus et al., 1987). Also both the circular dichroic and proton NMR spectra suggested the existence of great similarity of secondary structure (MacManus et al., 1984; Williams et al., 1987).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Banville, D., and Boie, Y., 1989. J. Mol. Biol., 207:481.
Berchtold, M. W., Epstein, P., Beaudet, A. L., Payne, M. E., Heizmann, C. W., and Means, A. R., 1987, J., Biol. Chem., 262:8696.
Bernaert, D., Brewer, L. M., MacManus, J. P., and Galand, P., 1989. Internat. J. Cancer, 43:719.
Brewer, L. M., Boynton, A. L., and MacManus, J. P., 1985. J. Nutr. Growth Cancer. 2:25.
Brewer, L. M., Gillen, M. F., and MacManus, J. P., 1989. Placenta. 10:359.
Brewer, L. M., and MacManus, J. P., 1985. Dev. Biol., 112:49.
Brewer, L. M., and MacManus, J. P., 1987. Placenta, 8:351.
Gillen, M. F., Banville, D., Rutledge, R. G., Narang, S., Seligy, V., Whitfield, J. F., and MacManus, J. P., 1987, J. Biol. Chem., 262:5308.
Gillen, M. F., Brewer, L. M., and MacManus, J. P., 1988. Cancer Lett., 40:151.
Henzl, M.T., and Birnbaum, E. R., 1988. J. Biol. Chem.,263:10674.
Henzl, M. T., Hapak, R. C., and Birnbaum, E. R., 1986. Biochim. Biophys. Acta. 872:16.
Hojman, F., and Peries, J., 1986. Ann. Inst. Pasteur /Virol., 137E:3.
Horowitz, M., Luria, S., Rechavi, G., and Givol, D., 1984, EMBO J., 13:2937.
Kuff,E.L., and Lueders, K.K., 1988. Adv. Cancer Res., 51:183.
MacManus, J. P., Brewer, L. M., and Gillen, M. F., 1987 In: “The Role of Calcium in Biological Systems”, Vol. IV L.J. Anghileri, ed., pp. 1–19, CRC Press, Boca Raton.
MacManus, J. P., Brewer, L. M., and Gillen, M. F., 1988, In: “Calcium and Calcium-Binding Proteins”, C. Gerday, R. Gilles, &L. Bolis, eds., pp. 128–138, Springer-Verlag, Berlin.
MacManus, J. P., Hutnik, C. M. L., Sykes, B. D., Szabo, A. G., Williams, T. C., and Banville, D., 1989, J. Biol. Chem., 264:3470.
MacManus, J. P., Szabo, A. G., and Williams, R. E., 1984. Biochem. J., 220:261.
Man, Y. M., Delius, H., and Leader, D. P., 1987. Nucl. Acids Res., 15:3291.
Moews, P. C., and Kretsinger, R. H., 1975. J. Mol. Biol., 91:201.
Mutus, B., Palmer, E. J., and MacManus, J. P., 1988. Biochemistry. 27:5615.
Ono, M., Toh, H., Miyata, T., and Awaya, T., 1985. J. Virol., 55:387.
Perret, C., Lomri, N., and Thomasset, M., 1988. J. Mol. Evol., 27:351,
Rossant, J., 1986, In: “Experimental Approaches to Mammalian Embryonic Development”, J. Rossant, &RA. Pedersen, eds., pp. 97–120, Cambridge University Press, Cambridge.
Sommer, E. W., and Heizmann, C. W., 1989. Cancer Res., 49:899.
Williams, T.C., Corson, D.C., Sykes, B.D., and MacManus, J. P., 1987. J. Biol. Chem., 262:6248.
Ymer, S., Tucker, W.Q.J., Sanderson, C. J., Hapel, A. J., Campbell, H.D., and Young, I.G., 1985, Nature. 317:255.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Plenum Press, New York
About this chapter
Cite this chapter
MacManus, J.P., Brewer, L.M., Banville, D. (1990). Oncomodulin in Normal and Transformed Cells. In: Pochet, R., Lawson, D.E.M., Heizmann, C.W. (eds) Calcium Binding Proteins in Normal and Transformed Cells. Advances in Experimental Medicine and Biology, vol 269. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5754-4_17
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5754-4_17
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5756-8
Online ISBN: 978-1-4684-5754-4
eBook Packages: Springer Book Archive