Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin.

@article{Jeffrey1998LigandinducedCC,
  title={Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin.},
  author={P. D. Jeffrey and Maria C. Bewley and RossT. A. Macgillivray and Anne B Mason and Robert C. Woodworth and Edward N Baker},
  journal={Biochemistry},
  year={1998},
  volume={37 40},
  pages={
          13978-86
        }
}
Serum transferrin binds ferric ions in the bloodstream and transports them to cells, where they are released in a process involving receptor-mediated endocytosis. Iron release is believed to be pH dependent and is coupled with a large conformational change. To help define the steps in iron release, we have determined the three-dimensional structure of the iron-free (apo) form of the recombinant N-lobe half-molecule of human serum transferrin (ApoTfN) by X-ray crystallography. Two crystal forms… CONTINUE READING

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