› 1le4

X-ray diffraction
2.5Å resolution

STRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HUMAN APOLIPOPROTEIN-E

Released:
DOI: 10.2210/pdb1le4/pdb
PDB entry 1le4 coloured by chain, front view.
PDB entry 1le4 coloured by chain, side view.
PDB entry 1le4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms.
Dong LM, Wilson C, Wardell MR, Simmons T, Mahley RW, Weisgraber KH, Agard DA
J Biol Chem 269 22358-65 (1994)
PMID: 8071364

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-135991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein E Chain: A
Molecule details ›
Chain: A
Length: 144 amino acids
Theoretical weight: 16.8 KDa
Source organism: Homo sapiens
Expression system: unidentified
UniProt:
  • Canonical: P02649 (Residues: 41-184; Coverage: 48%)
Gene name: APOE
Sequence domains: Apolipoprotein A1/A4/E domain
Structure domains: Apolipoprotein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 40.71Å b: 53.33Å c: 85.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 not available
Expression system: unidentified

Quick links

Citations

51 review citations

Apolipoprotein E: far more than a lipid transport protein.
Mahley et al. (2000)
50 more

6 mentions without citation

Apolipoprotein E: Structural Insights and Links to Alzheimer Disease Pathogenesis.
Chen et al. (2021)
5 more