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 Lettjournal_title
FEBS lettersauthors
Jamin N,Coïc YM,Landon C,Ovtracht L,Baleux F,Neumann JM,Sanson Adoi
10.1016/s0014-5793(02)03353-7keywords:
subject
Has Abstractpub_date
2002-10-09 00:00:00pages
256-60issue
2-3eissn
0014-5793issn
1873-3468pii
S0014579302033537journal_volume
529pub_type
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