The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion

@inproceedings{Giachin2015TheNC,
  title={The non-octarepeat copper binding site of the prion protein is a key regulator of prion
conversion},
  author={Gabriele Giachin and Phuong Thao Mai and Thanh Hoa Tran and Giulia Salzano and Federico Benetti and Valentina Migliorati and Alessandro Arcovito and Stefano della Longa and Giordano Mancini and Paola A. D’Angelo and Giuseppe Legname},
  booktitle={Scientific reports},
  year={2015}
}
The conversion of the prion protein (PrP(C)) into prions plays a key role in transmissible spongiform encephalopathies. Despite the importance for pathogenesis, the mechanism of prion formation has escaped detailed characterization due to the insoluble nature of prions. PrP(C) interacts with copper through octarepeat and non-octarepeat binding sites. Copper coordination to the non-octarepeat region has garnered interest due to the possibility that this interaction may impact prion conversion… CONTINUE READING
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