4hr9

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'''Unreleased structure'''
 
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The entry 4hr9 is ON HOLD until Paper Publication
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==Human interleukin 17A==
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<StructureSection load='4hr9' size='340' side='right'caption='[[4hr9]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4hr9]] is a 2 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=4HR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HR9 FirstGlance]. <br>
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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]] 2.48&#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=4hr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hr9 OCA], [https://pdbe.org/4hr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hr9 RCSB], [https://www.ebi.ac.uk/pdbsum/4hr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hr9 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The constituent polypeptides of the interleukin-17 family form six different homodimeric cytokines (IL-17A-F) and the heterodimeric IL-17A/F. Their interactions with IL-17 receptors A-E (IL-17RA-E) mediate host defenses while also contributing to inflammatory and autoimmune responses. IL-17A and IL-17F both preferentially engage a receptor complex containing one molecule of IL-17RA and one molecule of IL-17RC. More generally, IL-17RA appears to be a shared receptor that pairs with other members of its family to allow signaling of different IL-17 cytokines. Here we report crystal structures of homodimeric IL-17A and its complex with IL-17RA. Binding to IL-17RA at one side of the IL-17A molecule induces a conformational change in the second, symmetry-related receptor site of IL-17A. This change favors, and is sufficient to account for, the selection of a different receptor polypeptide to complete the cytokine-receptor complex. The structural results are supported by biophysical studies with IL-17A variants produced by site-directed mutagenesis.
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Authors: Liu, S.
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Crystal structures of interleukin 17A and its complex with IL-17 receptor A.,Liu S, Song X, Chrunyk BA, Shanker S, Hoth LR, Marr ES, Griffor MC Nat Commun. 2013;4:1888. doi: 10.1038/ncomms2880. PMID:23695682<ref>PMID:23695682</ref>
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Description: Human interleukin 17A
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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 4hr9" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Liu S]]

Current revision

Human interleukin 17A

PDB ID 4hr9

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