To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00263 [for PROSITE entry PS00291]

Prion protein signatures





Description

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|     |
 +---+----------------+--------------------|--------|----|+-----+
                                           +--------+    |
                                                         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.

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)


References

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
DOI10.1146/annurev.mi.43.100189.002021



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)