| Structural highlights
Publication Abstract from PubMed
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 sub-angstrom-resolution structure of a protofibril formed by a wild-type segment from the beta2-alpha2 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'.
Sub-angstrom cryo-EM structure of a prion protofibril reveals a polar clasp.,Gallagher-Jones M, Glynn C, Boyer DR, Martynowycz MW, Hernandez E, Miao J, Zee CT, Novikova IV, Goldschmidt L, McFarlane HT, Helguera GF, Evans JE, Sawaya MR, Cascio D, Eisenberg DS, Gonen T, Rodriguez JA Nat Struct Mol Biol. 2018 Jan 15. pii: 10.1038/s41594-017-0018-0. doi:, 10.1038/s41594-017-0018-0. PMID:29335561[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Gallagher-Jones M, Glynn C, Boyer DR, Martynowycz MW, Hernandez E, Miao J, Zee CT, Novikova IV, Goldschmidt L, McFarlane HT, Helguera GF, Evans JE, Sawaya MR, Cascio D, Eisenberg DS, Gonen T, Rodriguez JA. Sub-angstrom cryo-EM structure of a prion protofibril reveals a polar clasp. Nat Struct Mol Biol. 2018 Jan 15. pii: 10.1038/s41594-017-0018-0. doi:, 10.1038/s41594-017-0018-0. PMID:29335561 doi:http://dx.doi.org/10.1038/s41594-017-0018-0
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