Tumor necrosis factor receptor

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== Function ==
== Function ==
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'''Tumor necrosis factor receptor''' (TNFR) or '''death receptor''' is a trimeric cytokine receptor which binds TNF<ref>PMID:10358762</ref>. TNFR family contains several members and superfamily (TNFRSF) members. <br />
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'''Tumor necrosis factor receptor''' (TNFR) or '''death receptor''' is a trimeric cytokine receptor which binds TNF<ref>PMID:10358762</ref>. TNFR family contains several members and superfamily ('''TNFRSF''') members. <br />
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* '''TNFRSF 1''' is called '''Lymphotoxin-α or TNF-β''';<br />
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* '''TNFRSF 1''' is called '''Lymphotoxin-α or TNF-β'''<ref>PMID:20566898</ref>;<br />
* '''TNFRSF 3''' is called '''TNFR-III''';<br />
* '''TNFRSF 3''' is called '''TNFR-III''';<br />
* '''TNFRSF 4''' is called '''OX40L receptor''';<br />
* '''TNFRSF 4''' is called '''OX40L receptor''';<br />
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* '''TNFRSF 18''' is called '''GITRL''';<br />
* '''TNFRSF 18''' is called '''GITRL''';<br />
* '''TNFRSF 21''' is called '''Dr6''';<br />
* '''TNFRSF 21''' is called '''Dr6''';<br />
 +
* '''TNFRSF 25''' is called '''Dr3''';<br />
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See also
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*[[Tumor necrosis factor ligand superfamily]]
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*[[Cytokine receptors]]
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*[[Receptor]]
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*[[Immune receptors]]
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==See also [[Tumor necrosis factor ligand superfamily]]==
 
== Relevance ==
== Relevance ==
TRAPS - a condition characterized by recurrent episodes of fever is associated with TNFR<ref>PMID:24609716</ref>.
TRAPS - a condition characterized by recurrent episodes of fever is associated with TNFR<ref>PMID:24609716</ref>.
== Structural highlights ==
== Structural highlights ==
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The extracellular domain of TNFR contains 2 to 6 cysteine-rich domains (CRD). The <scene name='59/590824/Cv/5'>CRD domains are ca. 40 amino-acid long and contain 4-6 cysteine residues</scene>. The CRDs are involved in binding of TNF<ref>PMID:8939750</ref>. <scene name='59/590824/Cv/7'>Mg coordination site</scene>. Water molecules shown as red spheres.
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The extracellular domain of TNFR contains 2 to 6 cysteine-rich domains (CRD). The <scene name='59/590824/Cv/8'>CRD domains are ca. 40 amino-acid long and contain 4-6 cysteine residues</scene>. The CRDs are involved in binding of TNF<ref>PMID:8939750</ref>. <scene name='59/590824/Cv/9'>Mg coordination site</scene>. Water molecules are shown as red spheres.
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</StructureSection>
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==3D structures of tumor necrosis factor receptor==
==3D structures of tumor necrosis factor receptor==
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[[Tumor necrosis factor receptor 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Tumor necrosis factor receptor 1
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**[[1ncf]] – hTNFR-1 residues 12-172 (mutant) – human<br />
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**[[1ich]] – hTNFR-1 death domain (mutant) - NMR<br />
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**[[2eqp]] – hTNFR-1 residues 28-70 – NMR <br />
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**[[1ext]] – hTNFR-1 extracellular domain <br />
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**[[1ft4]] – hTNFR-1 extracellular domain + inhibitor<br />
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**[[3on9]] – evTNFR SECRET domain – ectromelia virus<br />
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**[[3ona]] – evTNFR SECRET domain + CX3CL1 <br />
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*Tumor necrosis factor receptor superfamily 1 (lymphotoxin-α, TNF-β)
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**[[1tnr]] – hTNFRSF-1 + TNFβ <br />
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**[[4mxv]] – hTNFSF-1 extracellular domain + antibody - human<BR />
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**[[4mxw]] – hTNFSF-1 extracellular domain + antibody + TNFR-III<BR />
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*Tumor necrosis factor receptor superfamily 1B
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**[[3alq]] – hTNFRSF-1B extracellular domain + TNF<br />
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*Tumor necrosis factor receptor superfamily-4 (OX40L receptor)
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**[[2hew]] – mTNFSF-4 extracellular domain - mouse<BR />
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**[[2hev]] – hTNFSF-4 extracellular domain + OX40 ligand<BR />
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**[[2hey]] – mTNFSF-4 extracellular domain + hOX40 ligand<BR />
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*Tumor necrosis factor receptor superfamily-5 (CD40L receptor)
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**[[1aly]] – hTNFSF-5 extracellular domain <BR />
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**[[1i9r]], [[5dmi]], [[5ihl]], [[6fax]] – hTNFSF-5 extracellular domain + antibody<BR />
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**[[5dmj]] – hTNFRSF-5 extracellular domain (mutant) + antibody<br />
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**[[3lkj]], [[5ihl]] – hTNFSF-5 extracellular domain + inhibitor<BR />
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**[[3qd6]] – hTNFRSF-5 extracellular domain + CD40 ligand<br />
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*Tumor necrosis factor receptor superfamily-6 (Fas)
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**[[3thm]], [[3tje]] – hTNFRSF-6 extracellular domain + antibody<br />
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**[[3ezq]] – hTNFRSF-6 Fas DD domain + FADD<br />
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**[[3oq9]] – mTNFRSF-6 Fas DD domain + FADD - mouse<br />
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*Tumor necrosis factor receptor superfamily-6B
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**[[3mhd]] – hTNFRSF-6B extracellular domain <br />
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**[[4msv]] – hTNFRSF-6B extracellular domain + hTNFRSF-6 extracellular domain<br />
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**[[4kgg]], [[4kgq]], [[4j6g]] – hTNFRSF-6B extracellular domain + hTNFRSF-14 extracellular domain<br />
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**[[3mi8]], [[3k51]] – hTNFRSF-6B extracellular domain + hTNFRSF-15 extracellular domain<br />
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**[[5l36]] – hTNFRSF-6B extracellular domain + hTNF ligand SF-6 extracellular domain<br />
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*Tumor necrosis factor receptor superfamily-9 (4-1BBL)
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**[[5wi8]], [[5wjf]] – hTNFSF-9 extracellular domain<BR />
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**[[2x29]], [[5wiw]] – hTNFSF-9 extracellular domain (mutant)<BR />
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**[[6cu0]], [[6cpr]], [[6bnv]] – hTNFSF-9 extracellular domain (mutant) + NSF ligand superfamily member 9<BR />
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*Tumor necrosis factor receptor superfamily-10B (Dr5)
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**[[2h9g]], [[4od2]], [[1za3]], [[3x3f]] – hTNFRSF-10B extracellular domain + antibody<br />
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**[[1d0g]] – hTNFRSF-10B extracellular domain + apoptosis-2 ligand<br />
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**[[1d4v]] – hTNFRSF-10B extracellular domain + TNF-related apoptosis inducing ligand<br />
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**[[4i9x]] – hTNFRSF-10B extracellular domain + UL141<br />
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**[[4n90]] – hTNFRSF-10B + hTNFRSF-10 + antibody <br />
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*Tumor necrosis factor receptor superfamily-11
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**[[1jtz]], [[1iqa]], [[1s55]] – mTNFSF-11 receptor-binding domain<BR />
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**[[3me2]], [[3qbq]], [[4giq]] – mTNFSF-11 receptor-binding domain + RANK <BR />
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*Tumor necrosis factor receptor superfamily-11A (RANK)
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**[[3me4]] – mTNFRSF-11A extracellular domain <br />
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**[[5bnq]] – mTNFRSF-11A extracellular domain + TNF ligand SF-11<br />
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*Tumor necrosis factor receptor superfamily-11B (Osteoprotegerin)
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**[[3urf]] – hTNFRSF-11B extracellular domain + RANKL<br />
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**[[4e4d]] – mTNFRSF-11B extracellular domain + RANKL<br />
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*TNFSF-12 superfamily member 12 (TWEAK)
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**[[4ht1]] – hTNFSF-12 extracellular domain + antibody<BR />
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*Tumor necrosis factor receptor superfamily-12A (TWEAKR)
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**[[2rpj]], [[2kmz]], [[2epq]] – hTNFRSF-12A cysteine-rich domain – NMR <br />
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*TNFSF-13B superfamily member 13B (BAFF, sTALL-1)
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**[[1jh5]], [[1kxg]], [[1kd7]], [[4zch]] – hTNFSF-13B extracellular domain <BR />
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**[[1oqd]] – hTNFSF-13B extracellular domain + B-cell maturation protein <BR />
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**[[1oqe]] – hTNFSF-13B extracellular domain + hTNFRSF-13C <BR />
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**[[4v46]] – hTNFSF-13B extracellular domain + hTNFRSF-13C + BAFF<BR />
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**[[1osg]], [[3v56]] – hTNFSF-13B extracellular domain + hTNFRSF-13C peptide <BR />
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**[[1xu1]] – hTNFRSF-13B extracellular domain + APRIL <br />
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*Tumor necrosis factor receptor superfamily-13C (BAFF receptor)
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**[[1osx]] – hTNFRSF-13C extracellular domain - NMR <br />
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**[[2hfg]] – hTNFRSF-13C cysteine-rich domain + antibody<BR />
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*Tumor necrosis factor receptor superfamily-14 (LIGHT)
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**[[4fhq]], [[4en0]] – hTNFRSF-14 extracellular domain <br />
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**[[2aw2]] – hTNFRSF-14 extracellular domain + B and T lymphocyte attenuator <br />
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**[[4rsu]] – hTNFRSF-14 extracellular domain + TNFRSF-14 ligand<br />
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**[[4kg8]] – hTNFSF-14 extracellular domain (mutant)<BR />
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**[[4j6g]] – hTNFSF-14 extracellular domain + DCR3 <BR />
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**[[4kgq]], [[4kgg]] – hTNFSF-14 extracellular domain (mutant) + DCR3 <BR />
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*Tumor necrosis factor receptor superfamily-16 (Low-affinity nerve growth factor receptor; p75NTR; p75 neurotrophin receptor)
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**[[4f42]], [[4f44]] – hTNFRSF-16 death domain<br />
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**[[2n97]] – hTNFRSF-16 death domain - NMR<br />
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**[[2mic]] – rTNFRSF-16 transmembrane domain – rat - NMR<br />
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**[[2mjo]] – rTNFRSF-16 transmembrane domain (mutant) - NMR<br />
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**[[1sg1]], [[3ij2]] – hTNFRSF-16 + beta nerve growth factor<br />
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**[[3buk]] – hTNFRSF-16 + neurotrophin-3<br />
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**[[2n80]] – hTNFRSF-16 death domain + rho GDP-dissociation inhibitor - NMR<br />
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**[[2n83]] – hTNFRSF-16 death domain + receptor interacting Ser/Thr protein kinase - NMR<br />
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*Tumor necrosis factor receptor superfamily-17
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**[[2kn1]] – hTNFRSF-17 extracellular domain - NMR <br />
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**[[4zfo]] – hTNFRSF-17 extracellular domain + antibody <br />
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**[[1xu2]] – hTNFRSF-17 extracellular domain + APRIL <br />
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*Tumor necrosis factor receptor superfamily-18 (GITRL)
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**[[4db5]] – TNFRSF-18 – rabbit <br />
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**[[4e4s]] – TNFRSF-18 – pika <br />
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**[[4g4f]] – TNFRSF-18 – bushbaby <br />
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**[[3fc0]], [[2qdn]], [[3b9i]] – mTNFRSF-18 <br />
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**[[2q1m]], [[3b93]], [[3b94]] – hTNFRSF-18 extracellular domain <br />
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**[[2r30]], [[2r32]] – hTNFRSF-18 extracellular domain (mutant) <br />
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*Tumor necrosis factor receptor superfamily-21 (Dr6)
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**[[3u3p]], [[3u3q]], [[3u3s]], [[3u3t]], [[3u3v]] – hTNFRSF-21 cysteine-rich domain<br />
 
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**[[2dbh]] – hTNFRSF-21 CARD-like domain - NMR<br />
 
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**[[3qo4]] – hTNFRSF-21 cysteine-rich domain<br />
 
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**[[4yn0]] – hTNFRSF-21 cysteine-rich domain + amyloid beta A4 protein<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Current revision

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

References

  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. ↑ Mounzer RH, Svendsen OS, Baluk P, Bergman CM, Padera TP, Wiig H, Jain RK, McDonald DM, Ruddle NH. Lymphotoxin-alpha contributes to lymphangiogenesis. Blood. 2010 Sep 23;116(12):2173-82. PMID:20566898 doi:10.1182/blood-2009-12-256065
  3. ↑ 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
  4. ↑ 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

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Michal Harel, Alexander Berchansky

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