› 2mgt

Solution NMR

Zinc induced dimer of the metal binding domain 1-16 of human amyloid beta-peptide with Alzheimer's disease pathogenic English mutation H6R

Released:
DOI: 10.2210/pdb2mgt/pdb
PDB entry 2mgt coloured by chain, ensemble of 20 models, front view.
PDB entry 2mgt coloured by chain, ensemble of 20 models, side view.
PDB entry 2mgt coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Interplay of histidine residues of the Alzheimer's disease Aβ peptide governs its Zn-induced oligomerization.
Istrate AN, Kozin SA, Zhokhov SS, Mantsyzov AB, Kechko OI, Pastore A, Makarov AA, Polshakov VI
Sci Rep 6 21734 (2016)
PMID: 26898943

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138395 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chains: A, B
Molecule details ›
Chains: A, B
Length: 18 amino acids
Theoretical weight: 2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-687; Coverage: 2%)
Gene names: A4, AD1, APP

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 40%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

10 review citations

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.
Nguyen et al. (2021)
9 more

5 mentions without citation

Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments.
Wild et al. (2017)
4 more