Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | PRION_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