Prion protein NMR structure and familial human spongiform encephalopathies.

@article{Riek1998PrionPN,
  title={Prion protein NMR structure and familial human spongiform encephalopathies.},
  author={Roland Riek and Gerhard Wider and Martin Urs Billeter and Simone Hornemann and Rudi Glockshuber and Kurt W{\"u}thrich},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 20},
  pages={11667-72}
}
The refined NMR structure of the mouse prion protein domain mPrP(121-231) and the recently reported NMR structure of the complete 208-residue polypeptide chain of mPrP are used to investigate the structural basis of inherited human transmissible spongiform encephalopathies. In the cellular form of mPrP no spatial clustering of mutation sites is observed that would indicate the existence of disease-specific subdomains. A hydrogen bond between residues 128 and 178 provides a structural basis for… CONTINUE READING

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