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Tumor necrosis factor receptor
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| - | <StructureSection load='1ext' size=' | + | <StructureSection load='1ext' size='350' side='right' caption='Structure of human TNFR extracellular domain complex with sulfate and Mg+2 ion (green) (PDB code [[1ext]]).' scene='' pspeed='8'> |
__TOC__ | __TOC__ | ||
== Function == | == Function == | ||
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* '''TNFRSF 6''' is called '''Fas''';<br /> | * '''TNFRSF 6''' is called '''Fas''';<br /> | ||
* '''TNFRSF 9''' is called '''4-1BBL''';<br /> | * '''TNFRSF 9''' is called '''4-1BBL''';<br /> | ||
| - | * '''TNFRSF | + | * '''TNFRSF 10''' see [[TRAIL]];<br /> |
* '''TNFRSF 10B''' is called '''Dr5''';<br /> | * '''TNFRSF 10B''' is called '''Dr5''';<br /> | ||
| - | * '''TNFRSF 11''' is called '''RANKL''';<br /> | ||
* '''TNFRSF 11A''' is called '''RANK''';<br /> | * '''TNFRSF 11A''' is called '''RANK''';<br /> | ||
* '''TNFRSF 11B''' is called '''Osteoprotegerin''';<br /> | * '''TNFRSF 11B''' is called '''Osteoprotegerin''';<br /> | ||
* '''TNFRSF 12''' is called '''TWEAK''';<br /> | * '''TNFRSF 12''' is called '''TWEAK''';<br /> | ||
* '''TNFRSF 12A''' is called '''TWEAKR''';<br /> | * '''TNFRSF 12A''' is called '''TWEAKR''';<br /> | ||
| - | * '''TNFRSF 13''' is called '''APRIL''';<br /> | ||
* '''TNFRSF 13B''' is called '''BAFF or sTALL-1''';<br /> | * '''TNFRSF 13B''' is called '''BAFF or sTALL-1''';<br /> | ||
* '''TNFRSF 13C''' is called '''BAFF receptor''';<br /> | * '''TNFRSF 13C''' is called '''BAFF receptor''';<br /> | ||
* '''TNFRSF 14''' is called '''LIGHT''';<br /> | * '''TNFRSF 14''' is called '''LIGHT''';<br /> | ||
| - | * '''TNFRSF 16''' is called ''' | + | * '''TNFRSF 16''' is called '''Low-affinity nerve growth factor receptor; p75NTR; p75 neurotrophin receptor''';<br /> |
* '''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 | ||
| + | *[[Tumor necrosis factor ligand superfamily]] | ||
| + | *[[Cytokine receptors]] | ||
| + | *[[Receptor]] | ||
| + | *[[Immune receptors]] | ||
| - | ==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 == | ||
| - | The extracellular domain of TNFR contains 2 to 6 cysteine-rich domains (CRD). | + | 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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==3D structures of tumor necrosis factor receptor== | ==3D structures of tumor necrosis factor receptor== | ||
| + | [[Tumor necrosis factor receptor 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | **[[3u3p]], [[3u3q]], [[3u3s]], [[3u3t]], [[3u3v]] – hTNFRSF-21 cysteine-rich domain<br /> | ||
| - | **[[2dbh]] – hTNFRSF-21 CARD-like domain - NMR<br /> | ||
| - | **[[3qo4]] – hTNFRSF-21 cysteine-rich domain<br /> | ||
| - | **[[4yn0]] – hTNFRSF-21 cysteine-rich domain + amyloid beta A4 protein<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category: Topic Page]] | [[Category: Topic Page]] | ||
Current revision
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References
- ↑ 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

