Tumor necrosis factor receptor
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TNFR/NGFR cysteine-rich region | |||||||||
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Structure of the soluble human 55 kd TNF receptor-human TNF beta complex.[1] | |||||||||
Identifiers | |||||||||
Symbol | TNFR_c6 | ||||||||
Pfam | PF00020 | ||||||||
InterPro | IPR011614 | ||||||||
PROSITE | PDOC00561 | ||||||||
SCOP | 1tnr | ||||||||
SUPERFAMILY | 1tnr | ||||||||
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A tumor necrosis factor receptor (TNFR), or death receptor, is a trimeric[2] cytokine receptor that binds tumor necrosis factors (TNF). The receptor cooperates with an adaptor protein (such as TRADD, TRAF, RIP), which is important in determining the outcome of the response (e.g. apoptosis, inflammation).
Because "TNF" is often used to describe TNF alpha, "TNFR" is often used to describe the receptors that bind to TNF alpha - namely, CD120. However, there are several other members of this family that bind to the other TNFs.[3][4]
Members
Family members include:[3]
Type | Protein | Aliases | Gene |
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1 (CD120) | CD120a | TNFRSF1A | |
CD120b | TNFRSF1B | ||
3 | Lymphotoxin β receptor | TNFRSF3 | LTBR |
4 | CD134 | TNFRSF4 | |
5 | CD40 | TNFRSF5 | CD40 |
6 | FAS | TNFRSF6 | FAS |
TNFRSF6B | TNFRSF6B | ||
7 | CD27 | TNFRSF7 | CD27 |
8 | CD30 | TNFRSF8 | |
9 | CD137 | TNFRSF9 | |
10 | TNFRSF10A | DR4 | TNFRSF10A |
TNFRSF10B | DR5 | TNFRSF10B | |
TNFRSF10C | TNFRSF10C | ||
TNFRSF10D | TNFRSF10D | ||
11 | RANK | TNFRSF11A | |
Osteoprotegerin | TNFRSF11B | ||
12 | TNFRSF12A | Fn14 | TNFRSF12A |
13 | TNFRSF13B | TNFRSF13B | |
TNFRSF13C | TNFRSF13C | ||
14 | TNFRSF14 | TNFRSF14 | |
16 | Nerve growth factor receptor | TNFRSF16 | NGFR |
17 | TNFRSF17 | TNFRSF17 | |
18 | TNFRSF18 | TNFRSF18 | |
19 | TNFRSF19 | TNFRSF19 | |
21 | TNFRSF21 | DR6 | TNFRSF21 |
25 | TNFRSF25 | DR3 TRAMP LARD WS-1[5] | TNFRSF25 |
27 | Ectodysplasin A2 receptor | TNFRSF27 | EDA2R |
References
- ↑ Banner DW, D'Arcy A, Janes W et al. (May 1993). "Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation". Cell 73 (3): 431–45. doi:10.1016/0092-8674(93)90132-A. PMID 8387891.
- ↑ Ashkenazi, A.; Dixit, VM (1998). "Death Receptors: Signaling and Modulation". Science 281 (5381): 1305–8. doi:10.1126/science.281.5381.1305. PMID 9721089.
- ↑ 3.0 3.1 Locksley RM, Killeen N, Lenardo MJ (2001). "The TNF and TNF receptor superfamilies: integrating mammalian biology". Cell 104 (4): 487–501. doi:10.1016/S0092-8674(01)00237-9. PMID 11239407.
- ↑ Hehlgans T, Pfeffer K (2005). "The intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: players, rules and the games". Immunology 115 (1): 1–20. doi:10.1111/j.1365-2567.2005.02143.x. PMC 1782125. PMID 15819693.
- ↑ Marsters. "Identification of a ligand for the death-domain-containing receptor Apo3". current biology. Retrieved 4 December 2013.
Further reading
- Kavurma MM, Tan NY, Bennett MR. (2008). "Death receptors and their ligands in atherosclerosis". Arterioscler Thromb Vasc Biol. 28 (10): 1694–702. doi:10.1161/ATVBAHA.107.155143. PMID 18669890.
- Hatano, E. (2007). "Tumor necrosis factor signaling in hepatocyte apoptosis". J Gastroenterol Hepatol. 22: S43–44. doi:10.1111/j.1440-1746.2006.04645.x. PMID 17567463.
External links
- Tumor Necrosis Factor Receptor at the US National Library of Medicine Medical Subject Headings (MeSH)
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