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Protein structure
The PrPSc differs from PrPC solely in conformation and is its isoform. The mature PrPC consists of approx. 208 amino acids, arranged as a disordered N-terminus and a globular C-terminal domain consisting of three α-helices and a short, antiparallel β-pleated sheet [1][2]. There is a GPI membrane anchor at the C-terminus that tethers the protein to cell membranes and proteins that are secreted and lacking the anchor component has been proven to be unaffected by the infectious isoform [3]. In contrast to the natural form of prion protein with only about 3 % of β-sheet secondary structure, the PrPSc form has about 47 % of the secondary structure in β-sheets [4] that create a core of four-rung β-solenoid fold [5].
References
- ↑ Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K. NMR solution structure of the human prion protein. Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):145-50. PMID:10618385
- ↑ Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K. NMR structure of the mouse prion protein domain PrP(121-321). Nature. 1996 Jul 11;382(6587):180-2. PMID:8700211 doi:10.1038/382180a0
- ↑ Chesebro B, Trifilo M, Race R, Meade-White K, Teng C, LaCasse R, Raymond L, Favara C, Baron G, Priola S, Caughey B, Masliah E, Oldstone M. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science. 2005 Jun 3;308(5727):1435-9. doi: 10.1126/science.1110837. PMID:15933194 doi:http://dx.doi.org/10.1126/science.1110837
- ↑ Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Mehlhorn I, Huang Z, Fletterick RJ, Cohen FE, et al.. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):10962-6. PMID:7902575
- ↑ Wille H, Requena JR. The Structure of PrP(Sc) Prions. Pathogens. 2018 Feb 7;7(1). pii: pathogens7010020. doi: 10.3390/pathogens7010020. PMID:29414853 doi:http://dx.doi.org/10.3390/pathogens7010020
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