The cellular prion protein binds copper in vivo

@article{Brown1997TheCP,
  title={The cellular prion protein binds copper in vivo},
  author={David R Brown and Kefeng Qin and Jochen Herms and Axel Madlung and Jean C Manson and Robert R Strome and Paul E. Fraser and Theo Kruck and Alex von Bohlen and Walter J. Schulz-Schaeffer and Armin Giese and David Westaway and Hans Kretzschmar},
  journal={Nature},
  year={1997},
  volume={390},
  pages={684-687}
}
The normal cellular form of prion protein (PrPC) is a precursor to the pathogenic protease-resistant forms (PrPSc) believed to cause scrapie, bovine spongiform encephalopathy (BSE) and Creutzfeldt–Jakob disease. Its amino terminus contains the octapeptide PHGGGWGQ, which is repeated four times and is among the best-preserved regions of mammalian PrPC. Here we show that the amino-terminal domain of PrPCexhibits five to six sites that bind copper (Cu(II)) presented as a glycine chelate. At… CONTINUE READING
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