1. Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant β-sheet structure
- Author
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Jean-Michel Neumann, Nadège Jamin, Alain Sanson, Céline Landon, Yves-Marie Coïc, Françoise Baleux, Ludmila Ovtracht, Service de Biophysique des Fonctions Membranaires, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Chimie Organique, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), and Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)
- Subjects
Models, Molecular ,Prions ,Protein Conformation ,[SDV]Life Sciences [q-bio] ,Molecular Sequence Data ,030303 biophysics ,Biophysics ,Beta sheet ,Scrapie ,Fibril ,Biochemistry ,Mice ,03 medical and health sciences ,Protein structure ,Structural Biology ,Spectroscopy, Fourier Transform Infrared ,Electron microscopy ,Genetics ,Animals ,Amino Acid Sequence ,Prion protein ,Infrared spectroscopy ,Nuclear Magnetic Resonance, Biomolecular ,Molecular Biology ,Peptide sequence ,030304 developmental biology ,Aggregate ,0303 health sciences ,Chemistry ,Cell Biology ,Microscopy, Electron ,Structural propensity ,Domain (ring theory) ,Helix ,Prion - Abstract
International audience; The conversion of the cellular prion protein into the beta-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 beta-sheet structures.
- Published
- 2002
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