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Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.
- Gallagher-Jones, Marcus;
- Glynn, Calina;
- Boyer, David R;
- Martynowycz, Michael W;
- Hernandez, Evelyn;
- Miao, Jennifer;
- Zee, Chih-Te;
- Novikova, Irina V;
- Goldschmidt, Lukasz;
- McFarlane, Heather T;
- Helguera, Gustavo F;
- Evans, James E;
- Sawaya, Michael R;
- Cascio, Duilio;
- Eisenberg, David S;
- Gonen, Tamir;
- Rodriguez, Jose A
- et al.
Published Web Location
https://doi.org/10.1038/s41594-017-0018-0Abstract
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'.
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