structure
HELIX 1 1 ASP 144 ASN 153 1 10
HELIX 2 2 GLN 172 LYS 194 1 23
HELIX 3 3 GLU 200 ALA 224 1 25
SHEET 1 S1 2 TYR 128 GLY 131 0
SHEET 2 S1 2 VAL 161 ARG 164 -1
SSBOND 1 CYS 179 CYS 214
function
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Bovine spongiform encephalopathy (BSE) and human
Creutzfeldt-Jakob disease (CJD) are among the most notable central nervous
system degenerative disorders caused by prions. CJD may present as a sporadic,
genetic, or infectious illness. Prions are transmissible particles that
are devoid of nucleic acid and seem to be composed exclusively of a modified
protein (PrPSc). The normal, cellular prion protein (PrPC) is converted
into PrPSc through a posttranslational process during which it acquires
a high beta-sheet content. It is thought that BSE is a result of cannibalism
in which faulty industrial practices produced prion-contaminated feed for
cattle. There is now considerable concern that bovine prions may have been
passed to humans,resulting in a new form of CJD.
script
-
zap
load "prion.pdb"
backbone on
select helix
ribbon
color structure
hbond on
select 179
select 214
script rotate
color yellow
spacefill 1.0
spacefill 1.3
spacefill 1.5
spacefill 1.7
spacefill 1.9
prion protein
![](prion1.gif)