› 1ioj

Solution NMR

HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES

Released:
DOI: 10.2210/pdb1ioj/pdb
PDB entry 1ioj coloured by chain, ensemble of 18 models, front view.
PDB entry 1ioj coloured by chain, ensemble of 18 models, side view.
PDB entry 1ioj coloured by chain, ensemble of 18 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformation of human apolipoprotein C-I in a lipid-mimetic environment determined by CD and NMR spectroscopy.
Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ
Biochemistry 38 14475-84 (1999)
PMID: 10545169

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-135994 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein C-I Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.64 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02654 (Residues: 27-83; Coverage: 100%)
Gene name: APOC1
Sequence domains: Apolipoprotein C-I (ApoC-1)
Structure domains: Apolipoprotein C-I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY AND SIMULATED ANNEALING
Expression system: Not provided

Quick links

Citations

9 review citations

Structural models of human apolipoprotein A-I: a critical analysis and review.
Brouillette et al. (2001)
8 more

7 mentions without citation

Amphipathic α-helices in apolipoproteins are crucial to the formation of infectious hepatitis C virus particles.
Fukuhara et al. (2014)
6 more