› 2llm

Solution NMR

Structure of amyloid precursor protein's transmembrane domain

Released:
DOI: 10.2210/pdb2llm/pdb
PDB entry 2llm coloured by chain, ensemble of 20 models, front view.
PDB entry 2llm coloured by chain, ensemble of 20 models, side view.
PDB entry 2llm coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural and dynamic study of the transmembrane domain of the amyloid precursor protein.
Nadezhdin KD, Bocharova OV, Bocharov EV, Arseniev AS
Acta Naturae 3 69-76 (2011)
PMID: 22649674

Function and Biology Details

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

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 42 Chain: A
Molecule details ›
Chain: A
Length: 43 amino acids
Theoretical weight: 4.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05067 (Residues: 686-726; Coverage: 5%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 79%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Understanding single-pass transmembrane receptor signaling from a structural viewpoint-what are we missing?
Bugge et al. (2016)
4 more

13 mentions without citation

Insights into the physiological function of the β-amyloid precursor protein: beyond Alzheimer's disease.
Dawkins et al. (2014)
12 more