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 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: 25395337DOI: 10.1002/anie.201408598 PDB entries with the same primary citation |
Experimental method | SOLID-STATE NMR |
Structure validation
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