Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.

ABSTRACT: Prion diseases are associated with the misfolding of the prion protein (PrP) from its normal cellular form (PrP^C ) to its infectious scrapie form (PrP^Sc ). Post-translational modifications in PrP in vivo can play an important role in modulating the process of misfolding. To gain more insight into the effects of post-translational modifications in PrP structure and dynamics and to test the hypothesis that such modifications can interact with the protein, we have performed molecular dynamics simulations of diglycosylated human PrP^C bound to a lipid bilayer via a glycophosphatidylinositol anchor. Multiple simulations were performed at three different pH ranges to explore pH effects on structure and dynamics. In contrast to simulations of protein-onl

SUBMITTER: Cheng CJ 

PROVIDER: S-EPMC5500178 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature