Advertisement

Lactoferrin pp 265-269 | Cite as

Crystallographic Studies on Metal and Anion Substituted Human Lactoferrin

  • Clyde A. Smith
  • Heather M. Baker
  • Musa S. Shongwe
  • Bryan F. Anderson
  • Edward N. Baker
Part of the Advances in, Experimental Medicine and Biology book series (AEMB, volume 357)

Abstract

The metal and anion binding function of the transferrins has been well characterised by a host of spectroscopic methods, and the members of this family of proteins are known to bind a wide variety of metal ions including the first, second and third row transition metals, the group 13 metals, the lanthanides and some of the actinides (Aisen and Harris, 1989). Crystallographic studies, on the other hand, have concentrated primarily on diferric and apolactoferrin (Anderson et al, 1989; 1990) and diferric rabbit transferrin (Bailey et al, 1988; Sarra et al, 1990). These crystallographic studies have defined the polypeptide chain folding and the metal (iron) and anion (carbonate) sites (Baker et al., this volume).

Keywords

Crystallographic Study Electron Donor Group Electron Spin Echo Envelope Modulation Sodium Oxalate Anion Binding 
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.

References

  1. Aisen, P. & Harris, D.C. (1989) in Iron Carriers and Iron Proteins (T. M. Loehr, Ed.) pp 241–351, VCH Publishers, New York.Google Scholar
  2. Aisen, P., Pinkowitz, R.A. & Leibman, A. (1974) Ann. N.Y. Acad. Sci. 222, 337.CrossRefGoogle Scholar
  3. Anderson, B.F., Baker, H.M., Noms, G.E., Rice, D.W. & Baker, E.N. (1989) J. Mol. Biol. 209, 711.PubMedCrossRefGoogle Scholar
  4. Anderson, B.F., Baker, H.M., Noms, G.E., Rumball, S.V., & Baker, E.N. (1990) Nature (London) 344, 784.CrossRefGoogle Scholar
  5. Bailey, S., Evans, R.W., Garratt, R.C., Gorinsky, B., Hasnain, S.S., Horsburgh, C., Jhoti, H., Lindley, P.F., Mydin, A., Sarra, R. & Watson, J.L. (1988) Biochemistry 27, 5804.PubMedCrossRefGoogle Scholar
  6. Dubach, J., Gaffney, B.J., More, K., Eaton, G.R. & Eaton, S.S. (1991) Biophys. J. 59, 1091.PubMedCrossRefGoogle Scholar
  7. Grossman, G., Appel, H., Hasnain, S.S., Neu, M., Schwab, F. & Thies, W.-G. (1991) Abstract from the 10th International Conference on Iron and Iron Proteins, Oxford, U.K.Google Scholar
  8. Norris, G.E., Baker, H.M. & Baker, E.N. (1989) J. Mol. Biol. 209, 329.PubMedCrossRefGoogle Scholar
  9. Sarra, R., Garratt, R., Gorinsky, B, Jhoti, H. & Lindley, P. (1990) Acta Cryst. B46, 763.Google Scholar
  10. Schlabach, M.R. & Bates, G.W. (1975) J. Biol. Chem. 250, 2182.PubMedGoogle Scholar
  11. Schneider, D.J., Roe, A.L., Mayer, R.J. & Que, L., Jr. (1984) J. Biol. Chem. 259, 9699.PubMedGoogle Scholar
  12. Smith, C.A., Anderson, B.F., Baker, H.M. and Baker, E.N. (1992) Biochemistry 31, 4527.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Clyde A. Smith
    • 1
  • Heather M. Baker
    • 1
  • Musa S. Shongwe
    • 1
  • Bryan F. Anderson
    • 1
  • Edward N. Baker
    • 1
  1. 1.Department of Chemistry and BiochemistryMassey UniversityPalmerston NorthNew Zealand

Personalised recommendations