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Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant β‐sheet structure
Author(s) -
Jamin Nadège,
Coı̈c Yves-Marie,
Landon Céline,
Ovtracht Ludmila,
Baleux Françoise,
Neumann Jean-Michel,
Sanson Alain
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03353-7
Subject(s) - fibril , beta sheet , scrapie , prion protein , sequence (biology) , peptide sequence , chemistry , globular protein , biophysics , protein secondary structure , protein structure , domain (mathematical analysis) , amino acid residue , helix (gastropod) , protein aggregation , biology , biochemistry , gene , medicine , mathematical analysis , ecology , mathematics , disease , pathology , snail
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.