Figures & data
Figure 1. Schematic representation of PrPC structural determinants. Highlighted: N-terminal domain (red line), globular domain (blue line), octarepeat region (OR) with octapeptide sequences (see main text), α-helices (H1, H2 and H3), β-strands (S1, S2), N-linked glycosylation sites (CHO), disulfide bridges (S-S) and glycosylphosphatidylinisotol (GPI) anchor.
![Figure 1. Schematic representation of PrPC structural determinants. Highlighted: N-terminal domain (red line), globular domain (blue line), octarepeat region (OR) with octapeptide sequences (see main text), α-helices (H1, H2 and H3), β-strands (S1, S2), N-linked glycosylation sites (CHO), disulfide bridges (S-S) and glycosylphosphatidylinisotol (GPI) anchor.](/cms/asset/c2905a4a-4a2f-43f0-a98e-5002510469f4/kprn_a_1022023_f0001_c.gif)
Figure 2. Cartoon of the major structural determinants and environmental key factors in prion protein folding and stability. Abbreviations correspond to: cellular prion protein (PrPC); prion (PrPSc); highly enthalpically stable intermediate state (IS); plasma membrane (PM); endosomial vesicles (EV); disulfide bridge (R-S-S-R); free thiol (R-SH).
![Figure 2. Cartoon of the major structural determinants and environmental key factors in prion protein folding and stability. Abbreviations correspond to: cellular prion protein (PrPC); prion (PrPSc); highly enthalpically stable intermediate state (IS); plasma membrane (PM); endosomial vesicles (EV); disulfide bridge (R-S-S-R); free thiol (R-SH).](/cms/asset/7295cd0b-0b07-4836-b438-eb3aca2a9158/kprn_a_1022023_f0002_c.gif)