Nature Cell Biology 7, 1039 - 1044 (2005)
doi:10.1038/ncb1105-1039
Prion domains: sequences, structures and interactionsEric D. Ross1, 2, Allen Minton1
& Reed B. Wickner11
Eric. D. Ross, Allen Minton and Reed B. Wickner are in the Laboratory of Biochemistry & Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA. wickner@helix.nih.gov
2
Eric D. Ross's present address is the Department of Biochemisry and Molecular Biology, Colorado State University, Ft. Collins, CO 80523, USA. Mammalian and most fungal infectious proteins (also known as prions) are self-propagating amyloid, a filamentous  -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 -sheet structure.
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