› 7q4m

Electron Microscopy
2.8Å resolution

Type II beta-amyloid 42 Filaments from Human Brain

Released:
DOI: 10.2210/pdb7q4m/pdb
PDB entry 7q4m coloured by chain, front view.
PDB entry 7q4m coloured by chain, side view.
PDB entry 7q4m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structures of amyloid-β 42 filaments from human brains.
Yang Y, Arseni D, Zhang W, Huang M, Lövestam S, Schweighauser M, Kotecha A, Murzin AG, Peak-Chew SY, Macdonald J, Lavenir I, Garringer HJ, Gelpi E, Newell KL, Kovacs GG, Vidal R, Ghetti B, Ryskeldi-Falcon B, Scheres SHW, Goedert M
Science 375 167-172 (2022)
PMID: 35025654
Related structures: EMD-13809

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 42 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: 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

1 bound ligand:
Ligand UNX 10 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.8Å
Relevant EMDB volumes: EMD-13809

Quick links

Citations

33 review citations

The molecular basis for cellular function of intrinsically disordered protein regions.
Holehouse et al. (2024)
32 more

15 mentions without citation

Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.
Yagi-Utsumi et al. (2022)
14 more