Prion glycoprotein: structure, dynamics, and roles for the sugars.

@article{Rudd2001PrionGS,
  title={Prion glycoprotein: structure, dynamics, and roles for the sugars.},
  author={Pauline M. Rudd and Mark R Wormald and David R. Wing and Stanley B Prusiner and Raymond A. Dwek},
  journal={Biochemistry},
  year={2001},
  volume={40 13},
  pages={3759-66}
}
The prion protein contains two N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The large size of the N-linked sugars, together with their dynamic properties, enables them to shield two orthogonal faces of the protein almost completely. Thus, the sugars can protect large regions of the protein surface from proteases and from nonspecific protein-protein interactions. Immunoprecipitation of prion protein with calnexin suggests that in the ER the oligosaccharides may… CONTINUE READING

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