Skip to main content
Fig. 1 | Microbial Cell Factories

Fig. 1

From: Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria

Fig. 1

Mouse PrP structure and domain organization. a Three dimensional structure of the globular domain of mouse PrP (only residues 124–226 are assigned by NMR), PDB: 1AG2. Alpha helices 1, 2 and 3 are represented in red; beta strands 1 and 2 in yellow; loops and turns in green. The dotted gray line represents the unstructured N-terminal domain, comprising residues 23–120 (figure done with PyMol and disordered domain drawn with Inkscape). b Scheme of the primary structure of mature murine PrP (residues 23–231). HD hydrophobic domain; β-sheets are depicted in yellow, α-helices in red, and the remaining of the C-terminal domain in green; N-181 and N-197 are sites of glycosylation; GPI glycosylphosphatidylinositol anchor; PK proteinase K cleavage site

Back to article page