Human prion protein pathogenic mutations

Fig. 1 Diagram of the human prion protein gene showing the octapeptide repeat region (51-91), regions of predicted secondary structure [designated a (helical) or [3 (sheet)], pathogenic or likely pathogenic mutations (above in red), non-synonymous polymorphisms and synonymous polymorphisms (below in green)...

Van der Kamp MW, Daggett V (2009) The consequences of pathogenic mutations to the human prion protein. Protein Eng Des Sel 22 461... 

Pathogenic mutations in the prion protein gene cause inherited prion disease. Approximately 15% of human... 

Prion and scrapie diseases are linked with the conformational transition of normally monomeric a-helical cellular prion protein, PrP, to a B-sheet-rich pathogenic form, PrP , which is prone to aggregation. A similar conformational transition of the normal cellular form of a-helical amyloid peptide (aAP (1-40)) into the disease-specific largely B-sheet form of amyloid peptide (BAP (1-40)) occurs in Alzheimer s disease, which results in amyloid deposits (Monaco et al., 2006). So far more than 19 different mutations in the human PrP gene have been linked with inherited prion diseases (Monaco et al., 2006). However, the molecular event triggering the spontaneous conversion of wild-type and... 

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