› 4i1l

X-ray diffraction
2.1Å resolution

Structural and Biological Features of FOXP3 Dimerization Relevant to Regulatory T Cell Function

Released:
DOI: 10.2210/pdb4i1l/pdb
PDB entry 4i1l coloured by chain, front view.
PDB entry 4i1l coloured by chain, side view.
PDB entry 4i1l coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural and biological features of FOXP3 dimerization relevant to regulatory T cell function.
Song X, Li B, Xiao Y, Chen C, Wang Q, Liu Y, Berezov A, Xu C, Gao Y, Li Z, Wu SL, Cai Z, Zhang H, Karger BL, Hancock WW, Wells AD, Zhou Z, Greene MI
Cell Rep 1 665-75 (2012)
PMID: 22813742

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Forkhead box protein P3 41 kDa form Chain: A
Molecule details ›
Chain: A
Length: 93 amino acids
Theoretical weight: 10.28 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99JB6 (Residues: 189-276; Coverage: 21%)
Gene name: Foxp3
Sequence domains: FOXP coiled-coil domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

3 bound ligands:
Ligand SO4 3 x SO4
Ligand MG 3 x MG
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P4322
Unit cell:
a: 37.13Å b: 37.13Å c: 135.672Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.236 0.289
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Regulatory T cells in autoimmune disease.
Dominguez-Villar et al. (2018)
24 more

3 mentions without citation

FoxP3 in Treg cell biology: a molecular and structural perspective.
Deng et al. (2020)
2 more