Tumor necrosis factor receptor

Function

Tumor necrosis factor receptor (TNFR) or death receptor is a trimeric cytokine receptor which binds TNF^[1]. TNFR family contains several members and superfamily (TNFRSF) members.

• TNFRSF 1 is called Lymphotoxin-α or TNF-β^[2];
  
• TNFRSF 3 is called TNFR-III;
  
• TNFRSF 4 is called OX40L receptor;
  
• TNFRSF 5 is called CD40L receptor;
  
• TNFRSF 6 is called Fas;
  
• TNFRSF 9 is called 4-1BBL;
  
• TNFRSF 10 see TRAIL;
  
• TNFRSF 10B is called Dr5;
  
• TNFRSF 11A is called RANK;
  
• TNFRSF 11B is called Osteoprotegerin;
  
• TNFRSF 12 is called TWEAK;
  
• TNFRSF 12A is called TWEAKR;
  
• TNFRSF 13B is called BAFF or sTALL-1;
  
• TNFRSF 13C is called BAFF receptor;
  
• TNFRSF 14 is called LIGHT;
  
• TNFRSF 16 is called Low-affinity nerve growth factor receptor; p75NTR; p75 neurotrophin receptor;
  
• TNFRSF 18 is called GITRL;
  
• TNFRSF 21 is called Dr6;
  
• TNFRSF 25 is called Dr3;
  

See also

• Tumor necrosis factor ligand superfamily
• Cytokine receptors
• Receptor
• Immune receptors

Relevance

TRAPS - a condition characterized by recurrent episodes of fever is associated with TNFR^[3].

Structural highlights

The extracellular domain of TNFR contains 2 to 6 cysteine-rich domains (CRD). The CRD domains are ca. 40 amino-acid long and contain 4-6 cysteine residues. The CRDs are involved in binding of TNF^[4]. Mg coordination site. Water molecules are shown as red spheres.

3D structures of tumor necrosis factor receptor

Tumor necrosis factor receptor 3D structures