The charge structure of helix 1 in the prion protein regulates conversion to pathogenic PrPSc.

@article{Norstrom2006TheCS,
  title={The charge structure of helix 1 in the prion protein regulates conversion to pathogenic PrPSc.},
  author={Eric M. Norstrom and James A. Mastrianni},
  journal={Journal of virology},
  year={2006},
  volume={80 17},
  pages={8521-9}
}
The prion diseases are transmissible neurodegenerative disorders linked to a pathogenic conformer (PrP(Sc)) of the normal prion protein (PrP(C)). Accumulation of PrP(Sc) occurs via a poorly defined process in which PrP(Sc) complexes with and converts endogenous PrP(C) to nascent PrP(Sc). Recent experiments have focused on the highly charged first alpha helix (H1) of PrP. It has been proposed that two putative asparagine-to-arginine intrahelical salt bridges stabilize H1 in PrP(C) yet form… CONTINUE READING

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