Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation**

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Schütz, Anne K, Vagt, Toni, Huber, Matthias, Ovchinnikova, Oxana Y, Cadalbert, Riccardo, Wall, Joseph, Güntert, Peter, Böckmann, Anja, Glockshuber, Rudi, Meier, Beat H
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2015
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4502972/
https://www.ncbi.nlm.nih.gov/pubmed/25395337
http://dx.doi.org/10.1002/anie.201408598
Descripción
Sumario: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.

Ejemplares similares