Prion protein NMR structures of cats, dogs, pigs, and sheep.
The NMR structures of the recombinant cellular form of the prion proteins (PrPC) 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, PrPC consists of an N-terminal flexibly extended tail with approximately 100 amino acid residues and a C-terminal globular domain of approximately 100 residues with three alpha-helices and a short antiparallel beta-sheet. Although this global architecture coincides with the previously reported murine, Syrian hamster, bovine, and human PrPC structures, there are local differences between the globular domains of the different species. Because the five newly determined PrPC structures originate from species with widely different transmissible spongiform encephalopathy records, the present data indicate previously uncharacterized possible correlations between local features in PrPC three-dimensional structures and susceptibility of different mammalian species to transmissible spongiform encephalopathies.
Lysek
Dominikus A
DA
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Zürich, CH-8093 Zürich, Switzerland.
Schorn
Christian
C
Nivon
Lucas G
LG
Esteve-Moya
Vicent
V
Christen
Barbara
B
Calzolai
Luigi
L
von Schroetter
Christine
C
Fiorito
Francesco
F
Herrmann
Torsten
T
Güntert
Peter
P
Wüthrich
Kurt
K
D000818:Animals; D002415:Cats; D004198:Disease Susceptibility; D004285:Dogs; D019906:Nuclear Magnetic Resonance, Biomolecular; D018621:PrPC Proteins / Q000737:chemistry; D017096:Prion Diseases / Q000209:etiology; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012756:Sheep; D013045:Species Specificity; D013552:Swine
D018621:PrPC Proteins; D011328:Prions