The prion protein gene: Identifying regulatory signals using marsupial sequence

Regulation of Prion Protein Expression by Noncoding Regions of the Prnp Gene

“…The finding that intron 1 has its own promoter activity and contributes to the full activity of the gene sequence is in agreement with previous studies of both the murine and the bovine Prnp gene. 10,21,27 However, these findings underestimated the role played by intron 1. The promoter activity present in intron 1 (exons construct) is as robust as the activity of the promoter construct in all cell lines (Table 1).…”

Human prion protein sequence elements impede cross-species chronic wasting disease transmission

“…The tertiary structure of PrP C is highly conserved among mammals; however, specific amino acid differences between species are hypothesized to impact the intermolecular binding of PrP C and PrP Sc (22). One segment of high sequence diversity is the β2-α2 loop, consisting of residues 165-175 (human numbering) in which only 3 amino acids (P165, Y169, and Q172) are strictly conserved (23,24).…”

New insights into structural determinants of prion protein folding and stability

“…Following the cleavage of an N-terminal signal peptide, PrP C is exported to the cell surface as a N-glycosylated protein. Its tridimensional structure is highly conserved among mammals, 11,12 and it is composed of a flexible unfolded N-terminal domain and an α-helical enriched globular domain (Figure 1). 13 The unfolded N-terminal domain consists of unusual glycine-rich repeats.…”