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

Academic Article
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Overview

authors

  • 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, Kurt

publication date

  • January 2005

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

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.

subject areas

  • Animals
  • Cats
  • Disease Susceptibility
  • Dogs
  • Nuclear Magnetic Resonance, Biomolecular
  • PrPC Proteins
  • Prion Diseases
  • Prions
  • Protein Conformation
  • Protein Structure, Secondary
  • Sheep
  • Species Specificity
  • Swine
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Research

keywords

  • feline transmissible spongiform encephalopathy
  • mammalian species
  • scrapie
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Identity

PubMed Central ID

  • PMC545531

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0408937102

PubMed ID

  • 15647367
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Additional Document Info

start page

  • 640

end page

  • 645

volume

  • 102

issue

  • 3

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