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-Structure paper
| タイトル | Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core. |
|---|---|
| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 27, Issue 5, Page 417-423, Year 2020 |
| 掲載日 | 2020年4月13日 |
著者 | 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 要旨 | 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. |
リンク | Nat Struct Mol Biol / PubMed:32284600 / PubMed Central |
| 手法 | EM (らせん対称) / X線回折 |
| 解像度 | 1.46 - 3.5 Å |
| 構造データ | EMDB-20900: human prion protein fibril, M129 variant ![]() PDB-6pq5: ![]() PDB-6pqa: |
| 化合物 | ![]() ChemComp-MLI: ![]() ChemComp-HOH: |
| 由来 |
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キーワード | PROTEIN FIBRIL / amyloid-like protofibril / amyloid / fibril / prion / filament / fiber / PrP |
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homo sapiens (ヒト)
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