The structure function relationship for the Prion protein

Abstract

Central to Prion diseases is the normal endogenous Prion protein, PrP C. In spite of years of research the exact function of this protein remains enigmatic. Numerous binding partners have been identified for PrP C and due to the presence of a repeated sequence of PHGGGWGQ in the proteins amino-terminus it can bind metal ions. The protein is a complex molecule and each portion of PrP C possesses different roles for function and/ or trafficking. As understanding the role of PrP C is central to these disorders the structure/function relationship will be reviewed here.

A nanoparticle-based immobilization assay for prion-kinetics study

“…The difference in the rate constants observed at this concentration may be associated with the difference in functional groups on the surface of the nanoparticles used. Prion protein is a complex entity, and although numerous binding partners have been found for the protein, its function still remains unclear, since each portion of the protein has its own functional properties [ 26 ]. Although significant effort has been made in elucidating prion related diseases, numerous questions on the structure and conformation of the protein are still to be answered.…”

The octarepeat region of hamster PrP (PrP51–91) enhances the formation of microtubule and antagonize Cu<sup>2+</sup>-induced microtubule-disrupting activity

“…The presence of Cu 2þ can confer different strains of prion disease with different protease resistance properties and can enhance reversibility of scrapie inactivation [30]. The endocytosis of PrP C is enhanced by its binding with Cu and zinc [31]. Through binding with divalent metal ions, PrP involves in the metabolism and transportation of these metal ions.…”