Deconvoluting the Cu2+ binding modes of full-length prion protein.

@article{Klewpatinond2008DeconvolutingTC,
  title={Deconvoluting the Cu2+ binding modes of full-length prion protein.},
  author={Mark Klewpatinond and Paul Davies and Suzanne Bowen and David R Brown and John H Viles},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 4},
  pages={1870-81}
}
The prion protein (PrP) is a cell-surface Cu(2+)-binding glycoprotein that when misfolded is responsible for a number of transmissible spongiform encephalopathies. Full-length PrP-(23-231) and constructs in which the octarepeat region has been removed, or His(95) and His(110) is replaced by alanine residues, have been used to elucidate the order and mode of Cu(2+) coordination to PrP-(23-231). We have built on our understanding of the appearance of visible CD spectra and EPR for various PrP… CONTINUE READING

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