Composition of pH-sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release.

@article{Halbrooks2005CompositionOP,
  title={Composition of pH-sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release.},
  author={Peter J Halbrooks and Anthony M. Giannetti and Joshua S. Klein and Pamela J. Bj{\"o}rkman and Julia R. Larouche and Valerie C. Smith and R. T. MacGillivray and Stephen J. Everse and Anne B Mason},
  journal={Biochemistry},
  year={2005},
  volume={44 47},
  pages={15451-60}
}
The transferrins (TF) are a family of bilobal glycoproteins that tightly bind ferric iron. Each of the homologous N- and C-lobes contains a single iron-binding site situated in a deep cleft. Human serum transferrin (hTF) serves as the iron transport protein in the blood; circulating transferrin binds to receptors on the cell surface, and the complex is internalized by endocytosis. Within the cell, a reduction in pH leads to iron release from hTF in a receptor-dependent process resulting in a… CONTINUE READING

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