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Prion domains: sequences, structures and interactions

Nature Cell Biology volume 7, pages 1039–1044 (2005)Cite this article

Abstract

Mammalian and most fungal infectious proteins (also known as prions) are self-propagating amyloid, a filamentous β-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 β-sheet structure.

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Figure 1: Classification of prions into four types.
Figure 2: Prion domains.
Figure 3: Sequence-independent prion formation argues for parallel β-sheet structure.

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  1. Eric D. Ross

    Present address: the Department of Biochemisry and Molecular Biology, Colorado State University, Ft. Collins, CO 80523, USA

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  1. the Laboratory of Biochemistry & Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, 20892-0830, MD, USA

    Eric D. Ross, Allen Minton & Reed B. Wickner

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Ross, E., Minton, A. & Wickner, R. Prion domains: sequences, structures and interactions. Nat Cell Biol 7, 1039–1044 (2005). https://doi.org/10.1038/ncb1105-1039

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