Prion protein NMR structures of cats, dogs, pigs, and sheep

Autor: Christine von Schroetter, Barbara Christen, Vicent Esteve-Moya, Christian Schorn, Dominikus A. Lysek, Lucas G. Nivón, Torsten Herrmann, Luigi Calzolai, Francesco Fiorito, Peter Güntert, Kurt Wüthrich
Rok vydání: 2005
Předmět:
Zdroj: Proceedings of the National Academy of Sciences of the United States of America. 102(3)
ISSN: 0027-8424
Popis: The NMR structures of the recombinant cellular form of the prion proteins (PrP C ) of the cat ( Felis catus ), dog ( Canis familiaris ), and pig ( Sus scrofa ), and of two polymorphic forms of the prion protein from sheep ( Ovis aries ) are presented. In all of these species, PrP C consists of an N-terminal flexibly extended tail with ≈100 amino acid residues and a C-terminal globular domain of ≈100 residues with three α-helices and a short antiparallel β-sheet. Although this global architecture coincides with the previously reported murine, Syrian hamster, bovine, and human PrP C structures, there are local differences between the globular domains of the different species. Because the five newly determined PrP C structures originate from species with widely different transmissible spongiform encephalopathy records, the present data indicate previously uncharacterized possible correlations between local features in PrP C three-dimensional structures and susceptibility of different mammalian species to transmissible spongiform encephalopathies.
Databáze: OpenAIRE