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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

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

doi

10.1016/s0014-5793(02)03353-7

keywords:

subject

Has Abstract

pub_date

2002-10-09 00:00:00

pages

256-60

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302033537

journal_volume

529

pub_type

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