5n9b
From Proteopedia
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<StructureSection load='5n9b' size='340' side='right'caption='[[5n9b]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5n9b' size='340' side='right'caption='[[5n9b]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5n9b]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5n9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N9B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5n9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n9b OCA], [https://pdbe.org/5n9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n9b RCSB], [https://www.ebi.ac.uk/pdbsum/5n9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n9b ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/I17RA_HUMAN I17RA_HUMAN] Defects in IL17RA are the cause of familial candidiasis type 5 (CANDF5) [MIM:[https://omim.org/entry/613953 613953]. CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.<ref>PMID:21350122</ref> |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/I17RA_HUMAN I17RA_HUMAN] Receptor for IL17A, IL17F and, in dimer with IL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling.<ref>PMID:21993848</ref> <ref>PMID:19838198</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Signaling through innate immune receptors such as the Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) superfamily proceeds via the assembly of large membrane-proximal complexes or "signalosomes." Although structurally distinct, the IL-17 receptor family triggers cellular responses that are typical of innate immune receptors. The IL-17RA receptor subunit is shared by several members of the IL-17 family. Using a combination of crystallographic, biophysical, and mutational studies, we show that IL-17A, IL-17F, and IL-17A/F induce IL-17RA dimerization. X-ray analysis of the heteromeric IL-17A complex with the extracellular domains of the IL-17RA and IL-17RC receptors reveals that cytokine-induced IL-17RA dimerization leads to the formation of a 2:2:2 hexameric signaling assembly. Furthermore, we demonstrate that the formation of the IL-17 signalosome potentiates IL-17-induced IL-36gamma and CXCL1 mRNA expression in human keratinocytes, compared with a dimerization-defective IL-17RA variant. | ||
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| + | IL-17-induced dimerization of IL-17RA drives the formation of the IL-17 signalosome to potentiate signaling.,Goepfert A, Barske C, Lehmann S, Wirth E, Willemsen J, Gudjonsson JE, Ward NL, Sarkar MK, Hemmig R, Kolbinger F, Rondeau JM Cell Rep. 2022 Oct 18;41(3):111489. doi: 10.1016/j.celrep.2022.111489. PMID:36260993<ref>PMID:36260993</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5n9b" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Interleukin receptor|Interleukin receptor]] | + | *[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Goepfert | + | [[Category: Goepfert A]] |
| - | [[Category: Rondeau | + | [[Category: Rondeau J-M]] |
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Revision as of 07:28, 3 November 2022
Crystal Structure of unliganded human IL-17RA
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