4nux

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==Structure of receptor A==
==Structure of receptor A==
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<StructureSection load='4nux' size='340' side='right' caption='[[4nux]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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<StructureSection load='4nux' size='340' side='right'caption='[[4nux]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nux]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NUX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nux]] 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=4NUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NUX FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nux OCA], [http://pdbe.org/4nux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nux RCSB], [http://www.ebi.ac.uk/pdbsum/4nux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nux ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.295&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nux OCA], [https://pdbe.org/4nux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nux RCSB], [https://www.ebi.ac.uk/pdbsum/4nux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nux ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/I17RA_HUMAN I17RA_HUMAN]] Defects in IL17RA are the cause of familial candidiasis type 5 (CANDF5) [MIM:[http://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>
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[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 ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interleukin 17 (IL-17) cytokines play a crucial role in mediating inflammatory and autoimmune diseases. A unique intracellular signaling domain termed SEFIR is found within all IL-17 receptors (IL-17Rs) as well as the key adaptor protein Act1. SEFIR-mediated protein-protein interaction is a crucial step in IL-17 cytokine signaling. Here, the 2.3 A resolution crystal structure of the SEFIR domain of IL-17RA, the most commonly shared receptor for IL-17 cytokine signaling, is reported. The structure includes the complete SEFIR domain and an additional alpha-helical C-terminal extension, which pack tightly together to form a compact unit. Structural comparison between the SEFIR domains of IL-17RA and IL-17RB reveals substantial differences in protein topology and folding. The uniquely long insertion between strand betaC and helix alphaC in IL-17RA SEFIR is mostly well ordered, displaying a helix (alphaCC'ins) and a flexible loop (CC'). The DD' loop in the IL-17RA SEFIR structure is much shorter; it rotates nearly 90 degrees with respect to the counterpart in the IL-17RB SEFIR structure and shifts about 12 A to accommodate the alphaCC'ins helix without forming any knots. Helix alphaC was identified as critical for its interaction with Act1 and IL-17-stimulated gene expression. The data suggest that the heterotypic SEFIR-SEFIR association via helix alphaC is a conserved and signature mechanism specific for IL-17 signaling. The structure also suggests that the downstream motif of IL-17RA SEFIR together with helix alphaC could provide a composite ligand-binding surface for recruiting Act1 during IL-17 signaling.
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Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved alpha-helix for Act1 binding and IL-17 signaling.,Zhang B, Liu C, Qian W, Han Y, Li X, Deng J Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1476-83. doi:, 10.1107/S1399004714005227. Epub 2014 Apr 30. PMID:24816115<ref>PMID:24816115</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4nux" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Interleukin receptor|Interleukin receptor]]
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*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Deng, J]]
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[[Category: Homo sapiens]]
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[[Category: Han, Y]]
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[[Category: Large Structures]]
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[[Category: Zhang, B]]
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[[Category: Deng J]]
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[[Category: Autoimmune inflammatory]]
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[[Category: Han Y]]
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[[Category: Cytokine]]
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[[Category: Zhang B]]
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[[Category: Immune system]]
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[[Category: Receptor]]
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[[Category: Sefir domain]]
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Current revision

Structure of receptor A

PDB ID 4nux

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