› 3r2p

X-ray diffraction
2.2Å resolution

2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals the Assembly of HDL by Dimerization.

Released:
DOI: 10.2210/pdb3r2p/pdb
PDB entry 3r2p coloured by chain, front view.
PDB entry 3r2p coloured by chain, side view.
PDB entry 3r2p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization.
Mei X, Atkinson D
J Biol Chem 286 38570-38582 (2011)
PMID: 21914797

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135985 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Truncated apolipoprotein A-I Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 21.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02647 (Residues: 25-208; Coverage: 74%)
Gene name: APOA1
Sequence domains: Apolipoprotein A1/A4/E domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21212
Unit cell:
a: 108.333Å b: 30.178Å c: 69.576Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.23 0.28
Expression system: Escherichia coli BL21(DE3)

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Citations

13 review citations

New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism.
Phillips MC. (2013)
12 more

33 mentions without citation

Peptide and protein nanoparticle conjugates: versatile platforms for biomedical applications.
Spicer et al. (2018)
32 more