Palindromic region of PrP is very important for prion protein aggregation.

The present study shows that the pathogenic mutations, G113V and A116V, in the palindromic region of moPrP may induce prion pathogenesis by accelerating misfolding and aggregation.

Both mutations are able to do this by inducing structure in the palindromic region, which appears to be a site for intermolecular association in the oligomers.

This study suggests that conformational conversion occurs in oligomeric protein.