Fig. 1
From: The biological function of the cellular prion protein: an update
Structural organization of PrPC. Schematic representation of mature mouse PrPC, showing protein domains, sites of post-translational modification, and binding sites for divalent cations and protein interactors of functional relevance. CC1 charge cluster 1, OR octapeptide repeats, CC2 charge cluster 2, HD hydrophobic domain, FT flexible tail, GD globular domain. Structurally defined domains are depicted by pink (α-helix) and green (β-strand) boxes. GPI glycosylphosphatidylinositol anchor, CHO glycosylation site, S-S disulfide bridge. α, β, and γ cleavage sites are indicated. Copper binding sites (Cu 2+) within and outside the octapeptide region are reported as well as the sites involved in the interaction with Aβ oligomers and with the G-protein-coupled receptor Adgrg6