Prion diseases are fatal transmissible neurodegenerative diseases. The normal prion protein (PrP) converts into a pathological aggregated form, PrPSc, which is enriched in the ß-sheet structure, however the structure of the converted form of PrP remains inaccessible to high resolution techniques. By designed tethering of selected secondary structure elements we show that separation and swapping of subdomains of the globular domain is necessary for conversion and that domain-swapped dimer of PrP precedes amyloid formation and represents a potential target for therapeutic intervention.
COBISS.SI-ID: 4602394