The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study.

@article{Nemeth2006TheNO,
  title={The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study.},
  author={Elizabeta Nemeth and Gloria Cuevas Preza and Chun-Ling Jung and Jerry Kaplan and Alan J. Waring and Tomas Ganz},
  journal={Blood},
  year={2006},
  volume={107 1},
  pages={
          328-33
        }
}
Hepcidin is the principal iron-regulatory hormone. It acts by binding to the iron exporter ferroportin, inducing its internalization and degradation, thereby blocking cellular iron efflux. The bioactive 25 amino acid (aa) peptide has a hairpin structure stabilized by 4 disulfide bonds. We synthesized a series of hepcidin derivatives and determined their bioactivity in a cell line expressing ferroportin-GFP fusion protein, by measuring the degradation of ferroportin-GFP and the accumulation of… CONTINUE READING

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