› 2m4j

Solid-state NMR

40-residue beta-amyloid fibril derived from Alzheimer's disease brain

Released:
DOI: 10.2210/pdb2m4j/pdb
PDB entry 2m4j coloured by chain, ensemble of 20 models, front view.
PDB entry 2m4j coloured by chain, ensemble of 20 models, side view.
PDB entry 2m4j coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue.
Lu JX, Qiang W, Yau WM, Schwieters CD, Meredith SC, Tycko R
Cell 154 1257-68 (2013)
PMID: 24034249

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo nonamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138405 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 40 amino acids
Theoretical weight: 4.34 KDa
Source organism: Homo sapiens
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: 4%
Refinement method: simulated annealing

Quick links

Citations

137 review citations

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
Chiti et al. (2017)
136 more

65 mentions without citation

Amyloid polymorphism: structural basis and neurobiological relevance.
Tycko R. (2015)
64 more