2MVX

Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation

Summary for 2MVX

• Entry DOI: 10.2210/pdb2mvx/pdb
• NMR Information: BMRB: 25289
• Descriptor: Amyloid beta A4 protein (1 entity in total)
• Functional Keywords: amyloid beta, osaka mutation, amyloid fibrils, protein fibril
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P05067
• Total number of polymer chains: 10
• Total formula weight: 42067.38

Authors

Schuetz, A.K.,Vagt, T.,Huber, M.,Ovchinnikova, O.Y.,Cadalbert, R.,Wall, J.,Guentert, P.,Bockmann, A.,Glockshuber, R.,Meier, B.H. (deposition date: 2014-10-17, release date: 2014-11-26, Last modification date: 2024-05-01)

Primary citation

Schutz, A.K.,Vagt, T.,Huber, M.,Ovchinnikova, O.Y.,Cadalbert, R.,Wall, J.,Guntert, P.,Bockmann, A.,Glockshuber, R.,Meier, B.H.
Atomic-Resolution Three-Dimensional Structure of Amyloid beta Fibrils Bearing the Osaka Mutation.
Angew.Chem.Int.Ed.Engl., 54:331-335, 2015

PubMed 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.

PubMed: 25395337
DOI: 10.1002/anie.201408598

Experimental method

SOLID-STATE NMR