Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29414853
&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215
Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29414853
.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Pathogens
2018 ; 7
(1
): ä Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
The Structure of PrP(Sc) Prions
#MMPMID29414853
Wille H
; Requena JR
Pathogens
2018[Feb]; 7
(1
): ä PMID29414853
show ga
PrP(Sc) (scrapie isoform of the prion protein) prions are the infectious agent
behind diseases such as Creutzfeldt-Jakob disease in humans, bovine spongiform
encephalopathy in cattle, chronic wasting disease in cervids (deer, elk, moose,
and reindeer), as well as goat and sheep scrapie. PrP(Sc) is an alternatively
folded variant of the cellular prion protein, PrP(C), which is a regular,
GPI-anchored protein that is present on the cell surface of neurons and other
cell types. While the structure of PrP(C) is well studied, the structure of
PrP(Sc) resisted high-resolution determination due to its general insolubility
and propensity to aggregate. Cryo-electron microscopy, X-ray fiber diffraction,
and a variety of other approaches defined the structure of PrP(Sc) as a four-rung
?-solenoid. A high-resolution structure of PrP(Sc) still remains to be solved,
but the four-rung ?-solenoid architecture provides a molecular framework for the
autocatalytic propagation mechanism that gives rise to the alternative
conformation of PrP(Sc). Here, we summarize the current knowledge regarding the
structure of PrP(Sc) and speculate about the molecular conversion mechanisms that
leads from PrP(C) to PrP(Sc).
free
free
free
