› 2mvx

Solid-state NMR

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

Released:
DOI: 10.2210/pdb2mvx/pdb
PDB entry 2mvx coloured by chain, ensemble of 20 models, front view.
PDB entry 2mvx coloured by chain, ensemble of 20 models, side view.
PDB entry 2mvx coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.
Schütz AK, Vagt T, Huber M, Ovchinnikova OY, Cadalbert R, Wall J, Güntert P, Böckmann A, Glockshuber R, Meier BH
Angew Chem Int Ed Engl 54 331-5 (2015)
PMID: 25395337

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 39 amino acids
Theoretical weight: 4.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05067 (Residues: 672-711; Coverage: 5%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 5%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

28 review citations

Supramolecular Hydrogelators and Hydrogels: From Soft Matter to Molecular Biomaterials.
Du et al. (2015)
27 more

31 mentions without citation

Implications of peptide assemblies in amyloid diseases.
Ke et al. (2017)
30 more