The synucleins are a family of redox-active copper binding proteins.

@article{Davies2011TheSA,
  title={The synucleins are a family of redox-active copper binding proteins.},
  author={P. R. Davies and Xiaoyan Wang and Claire J. Sarell and Alex Drewett and Frank Marken and John H Viles and David Renick Brown},
  journal={Biochemistry},
  year={2011},
  volume={50 1},
  pages={
          37-47
        }
}
Thermodynamic studies in conjunction with EPR confirm that α-synuclein, β-synuclein, and γ-synuclein bind copper(II) in a high affinity 1:1 stoichiometry. γ-Synuclein demonstrates the highest affinity, in the picomolar range, while α-synuclein and β-synuclein both bind copper(II) with nanomolar affinity. The copper center on all three proteins demonstrates reversible or partly reversible redox cycling. Various mutations show that the primary coordinating ligand for copper(II) is located within… CONTINUE READING

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