Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation

Cell. 1993 May 7;73(3):431-45. doi: 10.1016/0092-8674(93)90132-a.


The X-ray crystal structure of the complex of the extracellular domain of the human 55 kd tumor necrosis factor (TNF) receptor with human TNF beta has been determined at 2.85 A resolution. The complex has three receptor molecules bound symmetrically to one TNF beta trimer. The receptor fragment, a very elongated end to end assembly of four similar folding domains, binds in the groove between two adjacent TNF beta subunits. The structure of the complex defines the orientation of the ligand with respect to the cell membrane and provides a model for TNF receptor activation. The novel fold of the TNF receptor structure is likely to be representative of the nerve growth factor (NGF)/TNF receptor family as a whole.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Humans
  • Ligands
  • Lymphotoxin-alpha / chemistry*
  • Lymphotoxin-alpha / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Conformation*
  • Protein Structure, Secondary*
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / metabolism*
  • Receptors, Nerve Growth Factor / chemistry
  • Receptors, Tumor Necrosis Factor
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • X-Ray Diffraction


  • Ligands
  • Lymphotoxin-alpha
  • Receptors, Cell Surface
  • Receptors, Nerve Growth Factor
  • Receptors, Tumor Necrosis Factor
  • Recombinant Proteins