Tumor necrosis factor receptor

Revision as of 00:33, 13 October 2017 by Michal Harel (talk | contribs)

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;
  • 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 11 is called RANKL;
  • TNFRSF 11A is called RANK;
  • TNFRSF 11B is called Osteoprotegerin;
  • TNFRSF 12 is called TWEAK;
  • TNFRSF 12A is called TWEAKR;
  • TNFRSF 13 is called APRIL;
  • TNFRSF 13B is called BAFF or sTALL-1;
  • TNFRSF 13C is called BAFF receptor;
  • TNFRSF 14 is called LIGHT;
  • TNFRSF 16 is called Nerve growth factor receptor;
  • TNFRSF 18 is called GITRL;
  • TNFRSF 21 is called Dr6;

See also Tumor necrosis factor ligand superfamily

Relevance

TRAPS - a condition characterized by recurrent episodes of fever is associated with TNFR[2].

Structural highlights

The extracellular domain of TNFR contains 2 to 6 cysteine-rich domains (CRD). The . The CRDs are involved in binding of TNF[3]. . Water molecules shown as red spheres.

Structure of human TNFR extracellular domain complex with sulfate and Mg+2 ion (green) (PDB code 1ext).

Drag the structure with the mouse to rotate

3D structures of tumor necrosis factor receptor3D structures of tumor necrosis factor receptor

Updated on 13-October-2017

ReferencesReferences

  1. Wallach D, Varfolomeev EE, Malinin NL, Goltsev YV, Kovalenko AV, Boldin MP. Tumor necrosis factor receptor and Fas signaling mechanisms. Annu Rev Immunol. 1999;17:331-67. PMID:10358762 doi:http://dx.doi.org/10.1146/annurev.immunol.17.1.331
  2. Lopalco G, Rigante D, Vitale A, Frediani B, Iannone F, Cantarini L. Tumor necrosis factor receptor-associated periodic syndrome managed with the couple canakinumab-alendronate. Clin Rheumatol. 2015 Apr;34(4):807-9. doi: 10.1007/s10067-014-2556-8. Epub 2014, Mar 11. PMID:24609716 doi:http://dx.doi.org/10.1007/s10067-014-2556-8
  3. Naismith JH, Devine TQ, Kohno T, Sprang SR. Structures of the extracellular domain of the type I tumor necrosis factor receptor. Structure. 1996 Nov 15;4(11):1251-62. PMID:8939750

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky