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’. MicroED structure of a peptide from the β2–α2 loop of the bank vole prion protein reveals a protofibril stabilized by a dense network of hydrogen bonds.
Sub-ångstrom cryo-EM structure of a prion protofibril reveals a polar clasp
M. Gallagher-Jones,C. Glynn,D. Boyer,M. Martynowycz,Evelyn Hernandez,Jennifer Miao,Chih-Te Zee,I. Novikova,Lukasz Goldschmidt,Heather T Mcfarlane,G. Helguera,James E. Evans,M. Sawaya,D. Cascio,D. Eisenberg,T. Gonen,José A. Rodríguez
Published 2018 in Nature Structural & Molecular Biology
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- Publication year
2018
- Venue
Nature Structural & Molecular Biology
- Publication date
2018-01-15
- Fields of study
Biology, Medicine
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Semantic Scholar, PubMed
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