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7QKW

In vitro assembled 266-391 S356D tau filaments with KCl (44a)

Summary for 7QKW
Entry DOI10.2210/pdb7qkw/pdb
EMDB information14055
DescriptorMicrotubule-associated protein tau (1 entity in total)
Functional Keywordsalzheimer's disease, amyloid, tau, neurodegeneration, protein fibril
Biological sourceHomo sapiens (human)
Total number of polymer chains6
Total formula weight275519.23
Authors
Lovestam, S.,Scheres, S.H.W. (deposition date: 2021-12-19, release date: 2022-02-16, Last modification date: 2024-07-17)
Primary citationLovestam, 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: 35244536
DOI: 10.7554/eLife.76494
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.32 Å)
Structure validation

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数据于2024-11-13公开中

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