1. Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation.
- Author
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Schütz, Anne K., Vagt, Toni, Huber, Matthias, Ovchinnikova, Oxana Y., Cadalbert, Riccardo, Wall, Joseph, Güntert, Peter, Böckmann, Anja, Glockshuber, Rudi, and Meier, Beat H.
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GENETICS of Alzheimer's disease , *NUCLEAR magnetic resonance , *AMYLOID beta-protein , *DELETION mutation , *NEURODEGENERATION , *GENETICS - Abstract
Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ1-40 peptide with the Osaka mutation (E22Δ), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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