› 4jfn

X-ray diffraction
1.75Å resolution

Crystal structure of the N-terminal, growth factor-like domain of the amyloid precursor protein bound to copper

Released:
DOI: 10.2210/pdb4jfn/pdb
PDB entry 4jfn coloured by chain, front view.
PDB entry 4jfn coloured by chain, side view.
PDB entry 4jfn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Amyloid precursor protein dimerization and synaptogenic function depend on copper binding to the growth factor-like domain.
Baumkötter F, Schmidt N, Vargas C, Schilling S, Weber R, Wagner K, Fiedler S, Klug W, Radzimanowski J, Nickolaus S, Keller S, Eggert S, Wild K, Kins S
J Neurosci 34 11159-72 (2014)
PMID: 25122912

Function and Biology Details

Biochemical function:
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:
N-APP Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05067 (Residues: 23-185; Coverage: 22%)
Gene names: A4, AD1, APP
Sequence domains:
Structure domains: Amyloidogenic glycoprotein, heparin-binding domain

Ligands and Environments

2 bound ligands:
Ligand CU 1 x CU
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 34.05Å b: 49.07Å c: 66.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.23
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Not just amyloid: physiological functions of the amyloid precursor protein family.
Müller et al. (2017)
26 more

2 mentions without citation

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