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

Nadège Jamin 1 Yves-Marie Coïc 2 Céline Landon 3 Ludmila Ovtracht Françoise Baleux 2 Jean-Michel Neumann 1 Alain Sanson 1
1 Service de Biophysique des Fonctions Membranaires
2 UCO - Chimie Organique
3 CBM - Centre de biophysique moléculaire
Abstract : 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.
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Contributor : Françoise Baleux <>
Submitted on : Friday, August 10, 2007 - 4:39:04 PM
Last modification on : Tuesday, May 14, 2019 - 3:54:06 PM

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Nadège Jamin, Yves-Marie Coïc, Céline Landon, Ludmila Ovtracht, Françoise Baleux, et al.. Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant beta-sheet structure.. FEBS Letters, Wiley, 2002, 529 (2-3), pp.256-60. ⟨10.1016/S0014-5793(02)03353-7⟩. ⟨pasteur-00166871⟩

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