Prion domains: sequences, structures and interactions

Nat Cell Biol. 2005 Nov;7(11):1039-44. doi: 10.1038/ncb1105-1039.


Mammalian and most fungal infectious proteins (also known as prions) are self-propagating amyloid, a filamentous beta-sheet structure. A prion domain determines the infectious properties of a protein by forming the core of the amyloid. We compare the properties of known prion domains and their interactions with the remainder of the protein and with chaperones. Ure2p and Sup35p, two yeast prion proteins, can still form prions when the prion domains are shuffled, indicating a parallel in-register beta-sheet structure.

Publication types

  • Review

MeSH terms

  • Amyloid / chemistry*
  • Glutathione Peroxidase
  • Models, Biological
  • Molecular Chaperones / physiology*
  • Peptide Termination Factors
  • Prions / chemistry*
  • Prions / classification
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary*
  • Repetitive Sequences, Nucleic Acid
  • Saccharomyces cerevisiae Proteins / chemistry


  • Amyloid
  • Molecular Chaperones
  • Peptide Termination Factors
  • Prions
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Glutathione Peroxidase
  • URE2 protein, S cerevisiae