https://doi.org/10.15255/KUI.2012.39
Published: Kem. Ind. 63 (1-2) (2014) 11–18
Paper reference number: KUI-39/2012
Paper type: Review
Download paper:  PDF

Structural Studies of Prion Proteins

I. Biljan

Abstract

Misfolding of normal, cellular prion protein (PrPC) into a pathological form called prion or PrPSc is connected with a group of fatal neurodegenerative disorders known as prion diseases or transmissible spongiform encephalopathies. Molecular mechanism of prion formation still remains elusive and structural studies of both forms of PrP are very important for explaining the mechanism of protein misfolding in prion diseases. In some cases, prion diseases are caused by mutations in gene coding for PrP. Structural studies of PrP mutants may provide better understanding of early events of conformational changes during spontaneous formation of prions in inherited prion diseases. This paper gives an overview of the most important results of structural studies of PrPs with the emphasis on studies with PrP mutants performed by high-resolution NMR spectroscopy.

This work is licensed under a Creative Commons Attribution 4.0 International License

Keywords

prion protein, prions, structure, nuclear magnetic resonance, mutants