Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin.

@article{Davis1990MappingTB,
  title={Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin.},
  author={Lydia H. Davis and Vann Bennett},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 18},
  pages={10589-96}
}
This report describes initial characterization of the binding sites of ankyrin for spectrin and the anion exchanger using defined subfragments isolated from purified ankyrin domains. The spectrin-binding domain of ankyrin is comprised of two subdomains: an acidic, proline-rich region (pI = 4) involving the amino-terminal 80 residues from 828 to 908 and a basic region (pI = 8.8) that extends from 898 to 1386. The amino-terminal 70 amino acids of the spectrin-binding domain are critical for… CONTINUE READING

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