› 2jq3

Solution NMR

Structure and Dynamics of Human Apolipoprotein C-III

Released:
DOI: 10.2210/pdb2jq3/pdb
PDB entry 2jq3 coloured by chain, ensemble of 10 models, front view.
PDB entry 2jq3 coloured by chain, ensemble of 10 models, side view.
PDB entry 2jq3 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and dynamics of human apolipoprotein CIII.
Gangabadage CS, Zdunek J, Tessari M, Nilsson S, Olivecrona G, Wijmenga SS
J Biol Chem 283 17416-27 (2008)
PMID: 18408013

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135997 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein C-III Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02656 (Residues: 21-99; Coverage: 100%)
Gene name: APOC3
Sequence domains: Apolipoprotein CIII (Apo-CIII)
Structure domains: Apolipoprotein CIII

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 45%
Refinement method: simulated annealing, torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Apolipoprotein C-III and hepatic triglyceride-rich lipoprotein production.
Yao et al. (2012)
9 more

5 mentions without citation

Missense mutation in APOC3 within the C-terminal lipid binding domain of human ApoC-III results in impaired assembly and secretion of triacylglycerol-rich very low density lipoproteins: evidence that ApoC-III plays a major role in the formation of lipid precursors within the microsomal lumen.
Qin et al. (2011)
4 more