Prion protein NMR structures of chickens, turtles, and frogs.

  title={Prion protein NMR structures of chickens, turtles, and frogs.},
  author={Luigi Calzolai and Dominikus A Lysek and Daniel Roberto Perez and Peter G{\"u}ntert and Kurt W{\"u}thrich},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={102 3},
The NMR structures of the recombinant prion proteins from chicken (Gallus gallus; chPrP), the red-eared slider turtle (Trachemys scripta; tPrP), and the African clawed frog (Xenopus laevis; xlPrP) are presented. The amino acid sequences of these prion proteins show approximately 30% identity with mammalian prion proteins. All three species form the same molecular architecture as mammalian PrPC, with a long, flexibly disordered tail attached to the N-terminal end of a globular domain. The… CONTINUE READING


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