› 1ya9

X-ray diffraction
2.09Å resolution

Crystal Structure of the 22kDa N-Terminal Fragment of Mouse Apolipoprotein E

Released:
DOI: 10.2210/pdb1ya9/pdb
PDB entry 1ya9 coloured by chain, front view.
PDB entry 1ya9 coloured by chain, side view.
PDB entry 1ya9 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4.
Hatters DM, Peters-Libeu CA, Weisgraber KH
J Biol Chem 280 26477-82 (2005)
PMID: 15890642

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140038 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein E Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 21.05 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P08226 (Residues: 20-200; Coverage: 62%)
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
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 29.034Å b: 49.233Å c: 112.177Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.224
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Apolipoprotein E structure: insights into function.
Hatters et al. (2006)
6 more

5 mentions without citation

Structure-based reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions?
Collins et al. (2012)
4 more