› 1le2

X-ray diffraction
3Å resolution

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

Released:
DOI: 10.2210/pdb1le2/pdb
PDB entry 1le2 coloured by chain, front view.
PDB entry 1le2 coloured by chain, side view.
PDB entry 1le2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein.
Wilson C, Mau T, Weisgraber KH, Wardell MR, Mahley RW, Agard DA
Structure 2 713-8 (1994)
PMID: 7994571

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: 16.69 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: 41.06Å b: 53.94Å c: 83.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 not available
Expression system: unidentified

Quick links

Citations

15 review citations

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

6 mentions without citation

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