7QKW
In vitro assembled 266-391 S356D tau filaments with KCl (44a)
Summary for 7QKW
Entry DOI | 10.2210/pdb7qkw/pdb |
EMDB information | 14055 |
Descriptor | Microtubule-associated protein tau (1 entity in total) |
Functional Keywords | alzheimer's disease, amyloid, tau, neurodegeneration, protein fibril |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 6 |
Total formula weight | 275519.23 |
Authors | Lovestam, S.,Scheres, S.H.W. (deposition date: 2021-12-19, release date: 2022-02-16, Last modification date: 2024-07-17) |
Primary citation | Lovestam, S.,Koh, F.A.,van Knippenberg, B.,Kotecha, A.,Murzin, A.G.,Goedert, M.,Scheres, S.H.W. Assembly of recombinant tau into filaments identical to those of Alzheimer's disease and chronic traumatic encephalopathy. Elife, 11:-, 2022 Cited by PubMed Abstract: Abundant filamentous inclusions of tau are characteristic of more than 20 neurodegenerative diseases that are collectively termed tauopathies. Electron cryo-microscopy (cryo-EM) structures of tau amyloid filaments from human brain revealed that distinct tau folds characterise many different diseases. A lack of laboratory-based model systems to generate these structures has hampered efforts to uncover the molecular mechanisms that underlie tauopathies. Here, we report in vitro assembly conditions with recombinant tau that replicate the structures of filaments from both Alzheimer's disease (AD) and chronic traumatic encephalopathy (CTE), as determined by cryo-EM. Our results suggest that post-translational modifications of tau modulate filament assembly, and that previously observed additional densities in AD and CTE filaments may arise from the presence of inorganic salts, like phosphates and sodium chloride. In vitro assembly of tau into disease-relevant filaments will facilitate studies to determine their roles in different diseases, as well as the development of compounds that specifically bind to these structures or prevent their formation. PubMed: 35244536DOI: 10.7554/eLife.76494 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.32 Å) |
Structure validation
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