› 1osx

Solution NMR

Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3)

Released:
DOI: 10.2210/pdb1osx/pdb
PDB entry 1osx coloured by chain, ensemble of 20 models, front view.
PDB entry 1osx coloured by chain, ensemble of 20 models, side view.
PDB entry 1osx coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site.
Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA
Biochemistry 42 5977-83 (2003)
PMID: 12755599

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor necrosis factor receptor superfamily member 13C Chain: A
Molecule details ›
Chain: A
Length: 61 amino acids
Theoretical weight: 6.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96RJ3 (Residues: 1-61; Coverage: 33%)
Gene names: BAFFR, BR3, TNFRSF13C
Sequence domains: BAFF-R, TALL-1 binding

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics simulated annealing
Expression system: Escherichia coli

Quick links

Citations

12 review citations

BAFF, APRIL and their receptors: structure, function and signaling.
Bossen et al. (2006)
11 more