› 1eq1

Solution NMR

NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III

Released:
DOI: 10.2210/pdb1eq1/pdb
PDB entry 1eq1 coloured by chain, ensemble of 25 models, front view.
PDB entry 1eq1 coloured by chain, ensemble of 25 models, side view.
PDB entry 1eq1 coloured by chain, ensemble of 25 models, top view.
Source organism: Manduca sexta
Primary publication:
Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein.
Wang J, Sykes BD, Ryan RO
Proc Natl Acad Sci U S A 99 1188-93 (2002)
PMID: 11818551

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146531 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipophorin-3 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.41 KDa
Source organism: Manduca sexta
Expression system: Escherichia coli
UniProt:
  • Canonical: P13276 (Residues: 24-189; Coverage: 97%)
Sequence domains: Apolipophorin-III precursor (apoLp-III)
Structure domains: Apolipoprotein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

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Citations

11 review citations

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Rupprecht et al. (2010)
10 more

11 mentions without citation

Cholesterol transport in steroid biosynthesis: role of protein-protein interactions and implications in disease states.
Rone et al. (2009)
10 more