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Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.

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Nature Structural & Molecular Biology. 2018 Jan 15;. doi: 10.1038/s41594-017-0018-0
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Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp. Gonen Lab
Gallagher-Jones M, Glynn C, Boyer DR, Martynowycz MW, Hernandez E, Miao J, Zee C, Novikova IV, Goldschmidt L, McFarlane HT, Helguera GF, Evans JE, Sawaya MR, Cascio D, Eisenberg DS, Gonen T, Rodriguez JA
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Abstract

The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'.

PMID: 29335561 [PubMed - indexed for MEDLINE]

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