Accueil > Publications > Recherche par années > Années 2000 > 2002

Jamin, N ; Coic, YM ; Landon, C ; Ovtracht, L ; Baleux, F ; Neumann, JM ; Sanson, A

Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant ß-sheet structure

Febs Letters 529 (2-3) 256-260

par Administrateur - publié le

Abstract :

The conversion of the cellular prion protein into the ß-sheet-rich scrapie prion protein is thought to be the key step in the pathogenesis of prion diseases. To gain insight into this structural conversion, we analyzed the intrinsic structural propensity of the amino acid sequence of the murine prion C-terminal domain. For that purpose, this globular domain was dissected into its secondary structural elements and the structural propensity of the protein fragments was determined. Our results show that all these fragments, excepted that strictly encompassing helix 1, have a very high propensity to form structured aggregates with a dominant content of ß-sheet structures. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.