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2MVX

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

Summary for 2MVX
Entry DOI10.2210/pdb2mvx/pdb
NMR InformationBMRB: 25289
DescriptorAmyloid beta A4 protein (1 entity in total)
Functional Keywordsamyloid beta, osaka mutation, amyloid fibrils, protein fibril
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Single-pass type I membrane protein: P05067
Total number of polymer chains10
Total formula weight42067.38
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 citationSchutz, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLID-STATE NMR
Structure validation

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