Prion domains: sequences, structures and interactions.

Eric D Ross; Allen Minton; Reed B Wickner

doi:10.1038/ncb1105-1039

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Prion domains: sequences, structures and interactions.

Eric D Ross·Allen Minton·Reed B Wickner

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Abstract

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.

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Amyloid Glutathione Peroxidase Models, Biological Molecular Chaperones Peptide Termination Factors Prions Protein Conformation Protein Structure, Quaternary Protein Structure, Tertiary Repetitive Sequences, Nucleic Acid Saccharomyces cerevisiae Proteins Journal Article Review

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Eric D Ross, Allen Minton, Reed B Wickner. 2005. Prion domains: sequences, structures and interactions.. https://doi.org/10.1038/ncb1105-1039

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