› 1tkn

Solution NMR

Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein

Released:
DOI: 10.2210/pdb1tkn/pdb
PDB entry 1tkn coloured by chain, ensemble of 20 models, front view.
PDB entry 1tkn coloured by chain, ensemble of 20 models, side view.
PDB entry 1tkn coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein.
Dulubova I, Ho A, Huryeva I, Südhof TC, Rizo J
Biochemistry 43 9583-8 (2004)
PMID: 15274612

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble APP-beta Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 13.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P05067 (Residues: 460-569; Coverage: 15%)
Gene names: A4, AD1, APP
Sequence domains: E2 domain of amyloid precursor protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

The amyloid-beta precursor protein: integrating structure with biological function.
Reinhard et al. (2005)
6 more

8 mentions without citation

Copper binding to the Alzheimer's disease amyloid precursor protein.
Kong et al. (2008)
7 more