| Summary: | Prion protein family comprises proteins, which share not only similarity in their primary structure, but also similarity in their fold. These two groups of similarity presume a parceling in their respective biological function through the common biochemical properties. In this review, biochemical and structural similarities of PrP and two other proteins, Doppel and Shadoo, are evocated. Some evidence demonstrating respectively similarity between PrP N-terminal and C-terminal domain with respectively Shadoo and Doppel is presented. We extended primary structure similarity analysis to the other PrP subdomain as 166-176 polyNQ domain and compare it to proteins using aggregation as a support for structural information transference and structural epigenetic. Finally, we questioned if prion protein family have conserved the PrP structural bistability, which is in the origin of Prion phenomenon and if Prion pathology is not, ultimately, an exaptation of the physiological propensity of PrP to undergo a structural switch and polymerize
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