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• W4308732937 abstract "ABSTRACT The Arctic mutation, encoding E693G in the amyloid precursor protein (APP) gene [E22G in amyloid-β (Aβ)], causes dominantly inherited Alzheimer’s disease. Here we report the high-resolution cryo-EM structures of Aβ filaments from the frontal cortex of a previously described case ( AβPParc1 ) with the Arctic mutation. Most filaments consist of two pairs of non-identical protofilaments that comprise residues V12-V40 (human Arctic fold A) and E11-G37 (human Arctic fold B). They have a substructure (residues F20-G37) in common with the folds of type I and type II Aβ42. When compared to the structures of wild-type Aβ42 filaments, there are subtle conformational changes in the human Arctic folds, because of the lack of a side chain at G22, which may strengthen hydrogen bonding between mutant Aβ molecules and promote filament formation. A minority of Aβ42 filaments of type II was also present, as were tau paired helical filaments. In addition, we report the cryo-EM structures of Aβ filaments with the Arctic mutation from mouse knock-in line App NL-G-F . Most filaments are made of two identical mutant protofilaments that extend from D1-G37 (murine Arctic fold). In a minority of filaments, two dimeric folds pack against each other in an anti-parallel fashion. The murine Arctic fold differs from the human Arctic folds, but shares some substructure." @default.
• W4308732937 created "2022-11-15" @default.
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• W4308732937 date "2022-11-07" @default.
• W4308732937 modified "2023-10-01" @default.
• W4308732937 title "Cryo-EM Structures of Amyloid-β Filaments With the Arctic Mutation (E22G) From Human and Mouse Brains" @default.
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• W4308732937 doi "https://doi.org/10.1101/2022.11.07.515410" @default.
• W4308732937 hasPublicationYear "2022" @default.
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