› 8b9q

Solution NMR

Molecular structure of Cu(II)-bound amyloid-beta monomer implicated in inhibition of peptide self-assembly in Alzheimer's disease

Released:
DOI: 10.2210/pdb8b9q/pdb
PDB entry 8b9q coloured by chain, ensemble of 5 models, front view.
PDB entry 8b9q coloured by chain, ensemble of 5 models, side view.
PDB entry 8b9q coloured by chain, ensemble of 5 models, top view.
Source organism: Homo sapiens
Primary publication:
Molecular Structure of Cu(II)-Bound Amyloid-β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer's Disease.
Abelein A, Ciofi-Baffoni S, Mörman C, Kumar R, Giachetti A, Piccioli M, Biverstål H
OpenAccess logo JACS Au 2 2571-2584 (2022)
PMID: 36465548

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chain: A
Molecule details ›
Chain: A
Length: 40 amino acids
Theoretical weight: 4.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05067 (Residues: 672-711; Coverage: 5%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)

Ligands and Environments

1 bound ligand:
Ligand CU 1 x CU
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 26%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

APP-C31: An Intracellular Promoter of Both Metal-Free and Metal-Bound Amyloid-β40 Aggregation and Toxicity in Alzheimer's Disease.
Nam et al. (2024)
3 more

2 mentions without citation

Molecular Structure of Cu(II)-Bound Amyloid-β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer's Disease.
Abelein et al. (2022)
1 more