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

FEBS Letters

Coı̈c, Yves-Marie¹  Neumann, Jean-Michel²  Baleux, Françoise¹  Landon, Céline²  Ovtracht, Ludmila²  Sanson, Alain²  Jamin, Nadège² 

[1] Unité de Chimie Organique, URA CNRS 487, Institut Pasteur, 75724 Paris Cedex 15, France;CEA-Saclay, DBJC and URA CNRS 2096, Bât. 532, 91191 Gif sur Yvette Cedex, France

关键词: Prion;    Structural propensity;    Electron microscopy;    Infrared spectroscopy;    Aggregate;    Fibril;    PrPC;    cellular isoform of prion protein;    PrPSC;    scrapie isoform of prion protein;    ATR-FTIR;    attenuated total reflectance-Fourier transform infrared;    mPrP;    murine prion;   

DOI  :  10.1016/S0014-5793(02)03353-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The conversion of the cellular prion protein into the β-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 β-sheet structures.

【 授权许可】

Unknown