1XYQ

NMR structure of the pig prion protein

Summary for 1XYQ

• Entry DOI: 10.2210/pdb1xyq/pdb
• Related: 1XYJ 1XYK
• NMR Information: BMRB: 6380
• Descriptor: Major prion protein (1 entity in total)
• Functional Keywords: prion, prp, scprp, tse, unknown function
• Biological source: Sus scrofa (pig)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P49927
• Total number of polymer chains: 1
• Total formula weight: 12976.42

Authors

Lysek, D.A.,Schorn, C.,Herrmann, T.,Wuthrich, K. (deposition date: 2004-11-10, release date: 2005-01-04, Last modification date: 2024-10-30)

Primary citation

Lysek, D.A.,Schorn, C.,Nivon, L.G.,Esteve-Moya, V.,Christen, B.,Calzolai, L.,von Schroetter, C.,Fiorito, F.,Herrmann, T.,Guntert, P.,Wuthrich, K.
Prion protein NMR structures of cats, dogs, pigs, and sheep
Proc.Natl.Acad.Sci.Usa, 102:640-645, 2005

PubMed Abstract: 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.

PubMed: 15647367
DOI: 10.1073/pnas.0408937102

Experimental method

SOLUTION NMR