NR AFXJ
AU Jackson,G.S.
TI Spontaneous conformational change within the prion protein - implications for disease pathogenesis?
QU Bioessays 2001 Sep; 23(9): 772-4
PT journal article
AB A recent paper by Leclerc et al(1) describes how recombinant hamster prion protein can undergo a spontaneous change in conformation to a structure that has features in common with PrPsc. Structural change in the host prion protein, PrPc to an insoluble and aggregated form with increased beta-sheet content (PrPsc) is central to the pathology of prion diseases.(2) A detailed understanding of the nature of these conformational changes will increase our knowledge of the molecular basis of prion pathology. These findings may have implications for how the disease is initiated and provide a format for further investigation.
MH Animal; PrPc Proteins/chemistry/pathogenicity; PrPsc Proteins/chemistry/pathogenicity; Prion Diseases/*physiopathology; Prions/*chemistry/*pathogenicity; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins/chemistry; Scrapie/physiopathology
AD MRC Prion Unit, Department of Neurogenetics, Imperial College School of Medicine at St. Mary's, Norfolk Place, Paddington, London, W2 1NY, UK. g.s.jackson@ic.ac.uk
SP englisch
PO England