› 1mpv

Solution NMR

Structure of bhpBR3, the BAFF-binding loop of BR3 embedded in a beta-hairpin peptide

Released:
DOI: 10.2210/pdb1mpv/pdb
PDB entry 1mpv coloured by chain, ensemble of 20 models, front view.
PDB entry 1mpv coloured by chain, ensemble of 20 models, side view.
PDB entry 1mpv coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-kappaB2.
Kayagaki N, Yan M, Seshasayee D, Wang H, Lee W, French DM, Grewal IS, Cochran AG, Gordon NC, Yin J, Starovasnik MA, Dixit VM
Immunity 17 515-24 (2002)
PMID: 12387744

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
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: 14 amino acids
Theoretical weight: 1.59 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q96RJ3 (Residues: 24-24, 25-35; Coverage: 6%)
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: hybrid distance geometry/simulated annealing followed by restrained molecular dynamics.
Expression system: Not provided

Quick links

Citations

123 review citations

Signalling pathways of the TNF superfamily: a double-edged sword.
Aggarwal BB. (2003)
122 more