Molecular structure of serum transferrin at 3.3-A resolution.

@article{Bailey1988MolecularSO,
  title={Molecular structure of serum transferrin at 3.3-A resolution.},
  author={Steve Bailey and Robert Evans and Richard Garratt and Beatrice Gorinsky and S Samar Hasnain and C. Horsburgh and Harren Jhoti and Peter F. Lindley and A Mydin and R Sarra},
  journal={Biochemistry},
  year={1988},
  volume={27 15},
  pages={5804-12}
}
Serum transferrin is a metal-binding glycoprotein, molecular weight ca. 80,000, whose primary function is the transport of iron in the plasma of vertebrates. The X-ray crystallographic structure of diferric rabbit serum transferrin has been determined to a resolution of 3.3 A. The molecule has a beta alpha structure of similar topology to human lactoferrin and is composed of two homologous lobes that each bind a single ferric ion. Each lobe is further divided into two dissimilar domains, and… CONTINUE READING

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