PS00706

Prion protein signature 2

PROSITE patterns entry
Member databasePROSITE patterns
PROSITE patterns typeconserved site
Short namePRION_2

Description

Prion protein (PrP)
[1]
[3]
[2]
is a small glycoprotein found in high quantity in the brains of humans or animals infected with a number of degenerative neurological diseases such as Kuru, Creutzfeldt-Jacob disease (CJD), scrapie or bovine spongiform encephalopathy (BSE). PrP is encoded in the host genome and expressed both in normal and infected cells. It has a tendency to aggregate yielding polymers called rods. Structurally, PrP is a protein consisting of a signal peptide, followed by an N-terminal domain that contains tandem repeats of a short motif (PHGGGWGQ in mammals, PHNPGY in chicken), itself followed by a highly conserved domain of about 140 residues that contains a disulfide bond. Finally comes a C- terminal hydrophobic domain post-translationally removed when PrP is attached to the extracellular side of the cell membrane by a GPI-anchor. The structure of PrP is shown in the following schematic representation: +---+----------------+-******-------------------****-----+-----+ |Sig| Tandem repeats | C C S| | +---+----------------+--------------------|--------|----|+-----+ +--------+ | GPI 'C': conserved cysteine involved in a disulfide bond. '*': position of the patterns. As signature pattern for PrP, we selected a perfectly conserved alanine- and glycine-rich region of 16 residues as well as a region centered on the second cysteine involved in the disulfide bond.

References

1.Prions and prion proteins. Stahl N, Prusiner SB. FASEB J. 5, 2799-807, (1991). View articlePMID: 1916104

2.Scrapie prions. Prusiner SB. Annu. Rev. Microbiol. 43, 345-74, (1989). View articlePMID: 2572197

3.The scrapie agent and the prion hypothesis. Brunori M, Silvestrini MC, Pocchiari M. Trends Biochem. Sci. 13, 309-13, (1988). View articlePMID: 2908696

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