Yeast Prion Protein Structure Revealed

Prion proteins are linked to several diseases, including bovine spongiform encephalopathy in cattle, scrapie in sheep, and Creutzfeldt-Jakob disease in humans. Infectious prion-like proteins that also form amyloid fibrils are found in yeast and other fungi. Based on solid-state nuclear magnetic resonance data, Wasmer et al. provide a structural model of amyloid fibrils from the prion-forming domain of the fungal HET-s protein. An earlier preliminary model gave no information on intermolecular B-sheet propagation. The current model shows that the amyloid fibrils form a left-handed B-solenoid with two windings per molecule that is stabilized by hydrophobic and polar interactions and salt bridges.


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Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core. Wasmer et al. Science 14 March 2008: Vol. 319. no. 5869, pp. 1523 - 1526.