Tumor necrosis factor receptor

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Revision as of 11:51, 28 September 2016 by Michal Harel (talk | contribs)
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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. The extracellular domain of TNFR contains 2 to 6 cysteine-rich domains.

  • 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 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;


Disease

Relevance

Structural highlights

Structure of human TNFRSF-18 extracellular domain (PDB code 2q1m).

Drag the structure with the mouse to rotate

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

Updated on 28-September-2016

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

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

Michal Harel, Alexander Berchansky