PROSITE documentation PDOC00263
Prion protein signatures


Prion protein (PrP) [1,2,3] 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|     |
                                           +--------+    |
'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.

Last update:

November 1997 / Text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

PRION_1, PS00291; Prion protein signature 1  (PATTERN)

PRION_2, PS00706; Prion protein signature 2  (PATTERN)


1AuthorsStahl N. Prusiner S.B.
TitlePrions and prion proteins.
SourceFASEB J. 5:2799-2807(1991).
PubMed ID1916104

2AuthorsBrunori M. Chiara Silvestrini M.C. Pocchiari M.
TitleThe scrapie agent and the prion hypothesis.
SourceTrends Biochem. Sci. 13:309-313(1988).
PubMed ID2908696

3AuthorsPrusiner S.B.
TitleScrapie prions.
SourceAnnu. Rev. Microbiol. 43:345-374(1989).
PubMed ID2572197

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