Structural insights into the interaction between prion protein and nucleic acid.

@article{Lima2006StructuralII,
  title={Structural insights into the interaction between prion protein and nucleic acid.},
  author={Lu{\'i}s Maur{\'i}cio T R Lima and Yraima Cordeiro and Luzineide Wanderley Tinoco and Adriana Fonseca Marques and Cristiano L. P. de Oliveira and Srisailam Sampath and Ravindra B Kodali and Gildon Choi and Debora Foguel and Iris L. Torriani and Byron Caughey and Jerson L Silva},
  journal={Biochemistry},
  year={2006},
  volume={45 30},
  pages={9180-7}
}
The infectious agent of transmissible spongiform encephalopathies (TSE) is believed to comprise, at least in part, the prion protein (PrP). Other molecules can modulate the conversion of the normal PrP(C) into the pathological conformer (PrP(Sc)), but the identity and mechanisms of action of the key physiological factors remain unclear. PrP can bind to nucleic acids with relatively high affinity. Here, we report small-angle X-ray scattering (SAXS) and nuclear magnetic resonance spectroscopy… CONTINUE READING