Comparing the Folds of Prions and Other Pathogenic Amyloids.

ABSTRACT: Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt⁻Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-β(1-42) (Aβ(1-42)) fibrils, and α-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrP^Sc, is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrP^Sc as a 4-rung β-solenoid. Thus, the structure of PrP^Sc must have a high similarity to that of the fungal prion HET-s, whic

SUBMITTER: Flores-Fernandez JM 

PROVIDER: S-EPMC6027354 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature