› 8bfz

Electron Microscopy
2.8Å resolution

Amyloid-beta 42 filaments extracted from the human brain with Arctic mutation (E22G) of Alzheimer's disease | ABeta42

Released:
DOI: 10.2210/pdb8bfz/pdb
PDB entry 8bfz coloured by chain, front view.
PDB entry 8bfz coloured by chain, side view.
PDB entry 8bfz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structures of amyloid-β filaments with the Arctic mutation (E22G) from human and mouse brains.
Yang Y, Zhang W, Murzin AG, Schweighauser M, Huang M, Lövestam S, Peak-Chew SY, Saito T, Saido TC, Macdonald J, Lavenir I, Ghetti B, Graff C, Kumar A, Nordberg A, Goedert M, Scheres SHW
OpenAccess logo Acta Neuropathol (2023)
PMID: 36611124
Related structures: EMD-16022

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138402 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 42 Chains: A, B
Molecule details ›
Chains: A, B
Length: 42 amino acids
Theoretical weight: 4.52 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05067 (Residues: 672-713; Coverage: 6%)
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
Resolution: 2.8Å
Relevant EMDB volumes: EMD-16022

Quick links

Citations

3 review citations

Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids.
Scheres et al. (2023)
2 more