Three-Dimensional Structure of Lactoferrin

Implications for Function, Including Comparisons with Transferrin
  • Edward N. Baker
  • Bryan F. Anderson
  • Heather M. Baker
  • Ross T. A. MacGillivray
  • Stanley A. Moore
  • Neil A. Peterson
  • Steven C. Shewry
  • John W. Tweedie
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 443)


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.


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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  1. 1.
    Brock, J.H. (1985). In Metalloproteins (Harrison, P.M., ed.), Vol. 2, pp. 183–262, MacMillan London.Google Scholar
  2. 2.
    Baker, E.N. (1994). Adv. lnorg. Chem. 41, 389–463.Google Scholar
  3. 3.
    Birgens, H.S., Hansen, N.E., Karle, H. and Ostergaard Kristensen, L. (1983). Brit. J. Haematol 54, 383–391.CrossRefGoogle Scholar
  4. 4.
    Mann, D.M., Romm, E and Migliorini, M. (1994). J. Biol. Chem 269, 23661–23667.PubMedGoogle Scholar
  5. 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. 6.
    Hutchens, T.W., Maguson, Y.S. and Yip, T-T. (1989). Pediatr. Res. 26, 618–622.PubMedCrossRefGoogle Scholar
  7. 7.
    Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K. and Tornita, M. (1992). Biochim. Biophys. Acta 1121, 130–136.CrossRefGoogle Scholar
  8. 8.
    Baldwin, D.A., Jenny, R.R. and Aisen, P. (1984). J. Biol. Chem. 259, 13391–13394.PubMedGoogle Scholar
  9. 9.
    Mazurier, J. and Spik, G. (1980). Biochim. Biophys. Acta 629, 399–408.PubMedCrossRefGoogle Scholar
  10. 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. 11.
    Haridas, M., Anderson, B.F. and Baker, E.N. (1995). Acta Cryst D51, 629–646.Google Scholar
  12. 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. 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. 14.
    Moore, S.A., Anderson, B.F., Groom, C.R., Haridas, M. and Baker, E.N. (1997). Submitted for publication.Google Scholar
  15. 15.
    Day, C.L., Anderson, B.F., Tweedie, J.W. and Baker, E.N. (1993). J. Mol. Biol. 232, 1084–1100.PubMedCrossRefGoogle Scholar
  16. 16.
    Ward, P.P., Zhou, X. and Conneely, O.M. (1996). J. Biol. Chem. 271, 12790–12794.PubMedCrossRefGoogle Scholar
  17. 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. 18.
    Dewan, J.C., Mikami, B., Hirose, M. and Sacchettini, J.C. (1993). Biochemistry 32, 11963–11968.PubMedCrossRefGoogle Scholar
  19. 19.
    Smith, C.A., Anderson, B.F., Baker, H.M. and Baker, E.N. (1992). Biochemistry 31, 4527–4533.PubMedCrossRefGoogle Scholar
  20. 20.
    Smith, C.A., Anderson, B.F., Baker, H.M. and Baker, E.N. (1994). Acta Cryst. D50, 302–316.CrossRefGoogle Scholar
  21. 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. 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. 23.
    Morabito, M.A. and Moczydlowski, E. (1994). Proc. Natl. Acad. Sci. USA 91 2478–2482.PubMedCrossRefGoogle Scholar
  24. 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. 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. 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. 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. 28.
    Hocco, M.M., and Mowbray, S.L. (1994). J. Biol Chem 269, 8931–8936.Google Scholar
  29. 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. 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. 31.
    Egan, T.J., Zak, O. and Aisen, P. (1993). Biochemistry 32, 8162–8167.PubMedCrossRefGoogle Scholar
  32. 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

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Edward N. Baker
    • 1
  • Bryan F. Anderson
    • 1
  • Heather M. Baker
    • 1
  • Ross T. A. MacGillivray
    • 1
  • Stanley A. Moore
    • 1
  • Neil A. Peterson
    • 1
  • Steven C. Shewry
    • 1
  • John W. Tweedie
    • 1
  1. 1.Department of BiochemistryMassey UniversityPalmerston NorthNew Zealand

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