Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid
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- Anton Gorkovskiy
- Laboratories of aBiochemistry and Genetics and
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- Kent R. Thurber
- Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892
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- Robert Tycko
- Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892
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- Reed B. Wickner
- Laboratories of aBiochemistry and Genetics and
説明
<jats:title>Significance</jats:title> <jats:p>Infectious proteins (prions) are capable of encoding genetic information by templating their conformation, just as DNA templates its sequence. The mechanism of this templating has not been clear. We provide definitive proof that the architecture of amyloid of the prion domain of yeast prion protein Sup35p is a folded in-register parallel β-sheet, and our data identify some of the sites of folds in the sheet. This architecture naturally suggests a templating mechanism based on favorable interactions among aligned side chains of identical amino acids. This is the only mechanism suggested to date for such a conformation templating.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 111 (43), E4615-, 2014-10-13
Proceedings of the National Academy of Sciences
