Advances in Lactoferrin Research pp 1-14 | Cite as
Three-Dimensional Structure of Lactoferrin
Implications for Function, Including Comparisons with Transferrin
Chapter
Abstract
Lactoferrin has many demonstrated activities. Some of these undoubtedly correspond to important in vivo functions; others may only apply in vitro, but may nevertheless lead to possible uses for lactoferrin in medicine or in biotechnology. In either case, the key to understanding the molecular basis of these activities, and ultimately being able to manipulate them, resides in the three-dimensional structure of the protein.
Keywords
Iron Binding Iron Release Iron Site Human Transferrin Human Lactoferrin
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References
- 1.Brock, J.H. (1985). In Metalloproteins (Harrison, P.M., ed.), Vol. 2, pp. 183–262, MacMillan London.Google Scholar
- 2.Baker, E.N. (1994). Adv. lnorg. Chem. 41, 389–463.Google Scholar
- 3.Birgens, H.S., Hansen, N.E., Karle, H. and Ostergaard Kristensen, L. (1983). Brit. J. Haematol 54, 383–391.CrossRefGoogle Scholar
- 4.Mann, D.M., Romm, E and Migliorini, M. (1994). J. Biol. Chem 269, 23661–23667.PubMedGoogle Scholar
- 5.Elass-Rochard, E., Roseanu, A., Legrand, D., Trif, M., Salmon, V., Motas, C., Montreuil, J. and Spik, G. (1995). Biochem. J. 312, 839–845.PubMedGoogle Scholar
- 6.Hutchens, T.W., Maguson, Y.S. and Yip, T-T. (1989). Pediatr. Res. 26, 618–622.PubMedCrossRefGoogle Scholar
- 7.Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K. and Tornita, M. (1992). Biochim. Biophys. Acta 1121, 130–136.CrossRefGoogle Scholar
- 8.Baldwin, D.A., Jenny, R.R. and Aisen, P. (1984). J. Biol. Chem. 259, 13391–13394.PubMedGoogle Scholar
- 9.Mazurier, J. and Spik, G. (1980). Biochim. Biophys. Acta 629, 399–408.PubMedCrossRefGoogle Scholar
- 10.Anderson, B.F., Baker, H.M., Norris, G.E., Rice. D.W. and Baker, E.N. (1989). J. Mol. Biol. 209, 711–734.PubMedCrossRefGoogle Scholar
- 11.Haridas, M., Anderson, B.F. and Baker, E.N. (1995). Acta Cryst D51, 629–646.Google Scholar
- 12.Ward, P.P., Piddington, C.S., Cunningham, G.A., Zhou, Z., Wyatt, R.D. and Conneely, O.M. (1995). Bio/Technology 13, 489–503.Google Scholar
- 13.Pierce, A., Colavizza, D., Benaisser, M., Maes, P., Tartar, A., Montreuil, J. and Spik. G. (1991). Eur. J. Biochem. 196, 177–184.PubMedCrossRefGoogle Scholar
- 14.Moore, S.A., Anderson, B.F., Groom, C.R., Haridas, M. and Baker, E.N. (1997). Submitted for publication.Google Scholar
- 15.Day, C.L., Anderson, B.F., Tweedie, J.W. and Baker, E.N. (1993). J. Mol. Biol. 232, 1084–1100.PubMedCrossRefGoogle Scholar
- 16.Ward, P.P., Zhou, X. and Conneely, O.M. (1996). J. Biol. Chem. 271, 12790–12794.PubMedCrossRefGoogle Scholar
- 17.MacGillivray, R.T.A., Anderson, B.F., Brayer, G.D., Mason, A.B., Moore, S.A., Woodworth, R.C. and Baker, E.N. (1997). Manuscript in preparation.Google Scholar
- 18.Dewan, J.C., Mikami, B., Hirose, M. and Sacchettini, J.C. (1993). Biochemistry 32, 11963–11968.PubMedCrossRefGoogle Scholar
- 19.Smith, C.A., Anderson, B.F., Baker, H.M. and Baker, E.N. (1992). Biochemistry 31, 4527–4533.PubMedCrossRefGoogle Scholar
- 20.Smith, C.A., Anderson, B.F., Baker, H.M. and Baker, E.N. (1994). Acta Cryst. D50, 302–316.CrossRefGoogle Scholar
- 21.Baker, H.M., Anderson, B.F., Brodie, A.M., Shongwe, M.S., Smith, C.A., and Baker, E.N. (1996). Biochemistry 35, 9007–9013.PubMedCrossRefGoogle Scholar
- 22.Smith, C.A., Sutherland-Smith, A.J., Keppler, B.K., Kratz, F. and Baker, E.N. (1996). J. Biol. Inorg. Chem 1, 424–431.CrossRefGoogle Scholar
- 23.Morabito, M.A. and Moczydlowski, E. (1994). Proc. Natl. Acad. Sci. USA 91 2478–2482.PubMedCrossRefGoogle Scholar
- 24.Anderson, B.F., Baker, H.M., Norris, G.E., Rumball, S.V. and Baker, E.N. (1990). Nature 344, 784–787.PubMedCrossRefGoogle Scholar
- 25.Baker, E.N., Anderson, B.F., Baker, H.M., Faber, H.R., Smith, C.A. and Sutherland-Smith, A.J. (1997). In Lactoferrin: Interactions and Biological Functions (Hutchens, T.W. and Lonnerdal, B., eds), pp. 177–191, Humana Press, New Jersey.Google Scholar
- 26.Jameson, G.B., Breyer, W.E., Anderson, B.F., Day, C.L., Kingston, R.L. and Baker, E.N. (1997). Manuscript in preparation.Google Scholar
- 27.Jeffrey, P.J., Bewley, M.C., MacGillivray, R.T.A., Mason, A.B., Woodworth, R.C. and Baker, E.N. (1997). Manuscript in preparation.Google Scholar
- 28.Hocco, M.M., and Mowbray, S.L. (1994). J. Biol Chem 269, 8931–8936.Google Scholar
- 29.Faber, H.R., Bland, T., Day, C.L., Norris, G.E., Tweedie, J.W. and Baker, E.N. (1996). J. Mol. Biol. 256, 352–363.Google Scholar
- 30.Faber, H.R., Baker, C.J., Day, C.L., Tweedie, J.W. and Baker, E.N. (1996). Biochemistry 35, 14473–14479.PubMedCrossRefGoogle Scholar
- 31.Egan, T.J., Zak, O. and Aisen, P. (1993). Biochemistry 32, 8162–8167.PubMedCrossRefGoogle Scholar
- 32.Nicholson, H., Anderson, B.F., Bland, T., Shewry, S.C., Tweedie, J.W. and Baker, E.N. (1997) Biochemistry 36, 341–346.PubMedCrossRefGoogle Scholar
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