Abstract
Despite the great effort aimed at uncovering the physiological function of cellular prion protein, its role remains unclear. The highly conserved amino acid sequence of PrP indicates its important function, but normally developing PrP knockout mice and cattle were prepared. Here we propose hypothesis that prion protein has no function or a redundant one and more importantly, that the conserved amino acid sequence of mammalian PrPs is not the result of their important function, but rather due to cytotoxicity of most mutations occurring in the PrP molecule. It is possible that the majority of mutations in PrP dramatically destabilizes the PrP C structure and causes a pathological change in conformation, so that natural selection favours individuals with non-mutated PrP.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
