Prion Protein Domain PrP (121-231)

The prion protein PrP exists in two different conformational forms. PrPc is thought to be the benign form of the protein and is found in normal, healthy cells. However, PrPsc is thought to be the infectious "scrapie" form which causes neurodegenerative diseases such as bovine spongiform encephalopathy (BSE), Creutzfeldt-Jakob disease (CJD), kuru, and Gerstmann-Straussler syndrome. PrP is a scrapie-associated protein that accumulates in the brains of an animal infected with the scrapie agent, or in the brains of humans infected with the diseases just mentioned. Aggregates of PrP as large fibril protein structures are formed in the brains of infected organisms. However, in healthy organisms, the function of PrP is still not yet known.
PrP is a 208 amino-acid residue glycosylated protein which is connected to the cell's surface by a glycosyl phosphatidyl inositol anchor, or GPI-anchor. However, only 110 residues (121-231) of the PrP domain are shown here. The two glycosylation sites are Asn 181 and Asn 197, which are both shown in yellow. One disulfide bond is present in the protein (colored gold here) connecting the second and third helices via Cys179-Cys214. The protein is colored by secondary structure. Alpha helices=Magenta, beta sheets=Blue.

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