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-Structure paper
Title | Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 27, Issue 5, Page 417-423, Year 2020 |
Publish date | Apr 13, 2020 |
![]() | Calina Glynn / Michael R Sawaya / Peng Ge / Marcus Gallagher-Jones / Connor W Short / Ronquiajah Bowman / Marcin Apostol / Z Hong Zhou / David S Eisenberg / Jose A Rodriguez / ![]() |
PubMed Abstract | Self-templating assemblies of the human prion protein are clinically associated with transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a denaturant- and protease- ...Self-templating assemblies of the human prion protein are clinically associated with transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a denaturant- and protease-resistant fibril formed in vitro spontaneously by a 9.7-kDa unglycosylated fragment of the human prion protein. This human prion fibril contains two protofilaments intertwined with screw symmetry and linked by a tightly packed hydrophobic interface. Each protofilament consists of an extended beta arch formed by residues 106 to 145 of the prion protein, a hydrophobic and highly fibrillogenic disease-associated segment. Such structures of prion polymorphs serve as blueprints on which to evaluate the potential impact of sequence variants on prion disease. |
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Methods | EM (helical sym.) / X-ray diffraction |
Resolution | 1.46 - 3.5 Å |
Structure data | EMDB-20900: human prion protein fibril, M129 variant ![]() PDB-6pq5: ![]() PDB-6pqa: |
Chemicals | ![]() ChemComp-MLI: ![]() ChemComp-HOH: |
Source |
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![]() | PROTEIN FIBRIL / amyloid-like protofibril / amyloid / fibril / prion / filament / fiber / PrP |