Generating Bona Fide Mammalian Prions with Internal Deletions.

ABSTRACT:

Unlabelled

Mammalian prions are PrP proteins with altered structures causing transmissible fatal neurodegenerative diseases. They are self-perpetuating through formation of beta-sheet-rich assemblies that seed conformational change of cellular PrP. Pathological PrP usually forms an insoluble protease-resistant core exhibiting beta-sheet structures but no more alpha-helical content, loosing the three alpha-helices contained in the correctly folded PrP. The lack of a high-resolution prion structure makes it difficult to understand the dynamics of conversion and to identify elements of the protein involved in this process. To determine whether completeness of residues within the protease-resistant domain is required for prions, we performed serial deletions in the helix H2 C terminus

SUBMITTER: Munoz-Montesino C 

PROVIDER: S-EPMC4944278 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature