› 1o8t

Solution NMR

Global Structure and Dynamics of Human Apolipoprotein CII in Complex with Micelles: Evidence for increased mobility of the helix involved in the activation of lipoprotein lipase

Released:
DOI: 10.2210/pdb1o8t/pdb
PDB entry 1o8t coloured by chain, ensemble of 68 models, front view.
PDB entry 1o8t coloured by chain, ensemble of 68 models, side view.
PDB entry 1o8t coloured by chain, ensemble of 68 models, top view.
Source organism: Homo sapiens
Primary publication:
Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase.
Zdunek J, Martinez GV, Schleucher J, Lycksell PO, Yin Y, Nilsson S, Shen Y, Olivecrona G, Wijmenga S
Biochemistry 42 1872-89 (2003)
PMID: 12590574

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein C-II Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02655 (Residues: 23-101; Coverage: 100%)
Gene names: APC2, APOC2
Sequence domains: Apolipoprotein C-II
Structure domains: Apolipoprotein C-II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: RESTRAINT MOLECULAR DYNAMICS
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Lipolysis: pathway under construction.
Zechner et al. (2005)
9 more

1 mention without citation

Lipase-Secreting Bacillus Species in an Oil-Contaminated Habitat: Promising Strains to Alleviate Oil Pollution.
Lee et al. (2015)