Disulfide-crosslink scanning reveals prion-induced conformational changes and prion strain-specific structures of the pathological prion protein PrP^Sc.

ABSTRACT: Prions are composed solely of the pathological isoform (PrP^Sc) of the normal cellular prion protein (PrP^C). Identification of different PrP^Sc structures is crucially important for understanding prion biology because the pathogenic properties of prions are hypothesized to be encoded in the structures of PrP^Sc However, these structures remain yet to be identified, because of the incompatibility of PrP^Sc with conventional high-resolution structural analysis methods. Previously, we reported that the region between the first and the second α-helix (H1∼H2) of PrP^C might cooperate with the more C-terminal side region for efficient interactions with PrP^Sc From this starting point, we created a series of PrP variants with

SUBMITTER: Taguchi Y 

PROVIDER: S-EPMC6102138 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature