The atomic structure of the infectious, protease-resistant, beta-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the subangstrom-resolution structure of a protofibril formed by a wild-type segment from the beta 2-alpha 2 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'.
Published: February 4, 2022
Citation
Gallagher-Jones M., C. Glynn, D.R. Boyer, M.W. Martynowycz, E. Hernandez, J. Miao, and C. Zee, et al. 2018.Sub-angstrom cryo-EM structure of a prion protofibril reveals a polar clasp.Nature Structural & Molecular Biology 25, no. 2:131-134.PNNL-SA-133752.doi:10.1038/s41594-017-0018-0