Tumor necrosis factor receptor
FunctionTumor 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.
RelevanceTRAPS - a condition characterized by recurrent episodes of fever is associated with TNFR[2]. Structural highlightsThe 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[3]. |
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3D structures of tumor necrosis factor receptor3D structures of tumor necrosis factor receptor
Updated on 28-September-2016
ReferencesReferences
- ↑ 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
- ↑ 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
- ↑ 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