3wo3

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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wo2|3wo2]], [[3wo4|3wo4]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wo2|3wo2]], [[3wo4|3wo4]]</td></tr>
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<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=3wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wo3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wo3 RCSB], [http://www.ebi.ac.uk/pdbsum/3wo3 PDBsum]</span></td></tr>
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<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=3wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wo3 OCA], [http://pdbe.org/3wo3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wo3 RCSB], [http://www.ebi.ac.uk/pdbsum/3wo3 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/IL18_HUMAN IL18_HUMAN]] Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. [[http://www.uniprot.org/uniprot/IL18R_HUMAN IL18R_HUMAN]] Receptor for interleukin 18 (IL-18). Binding to the agonist leads to the activation of NF-kappa-B.
[[http://www.uniprot.org/uniprot/IL18_HUMAN IL18_HUMAN]] Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. [[http://www.uniprot.org/uniprot/IL18R_HUMAN IL18R_HUMAN]] Receptor for interleukin 18 (IL-18). Binding to the agonist leads to the activation of NF-kappa-B.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation. The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease. IL-18 forms a signalling complex with the IL-18 receptor alpha (Ralpha) and beta (Rbeta) chains at the plasma membrane, which induces multiple inflammatory cytokines. Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains. Generally, the receptors' recognition mode for IL-18 is similar to IL-1beta; however, certain notable differences were observed. The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode. The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
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The structural basis for receptor recognition of human interleukin-18.,Tsutsumi N, Kimura T, Arita K, Ariyoshi M, Ohnishi H, Yamamoto T, Zuo X, Maenaka K, Park EY, Kondo N, Shirakawa M, Tochio H, Kato Z Nat Commun. 2014 Dec 15;5:5340. doi: 10.1038/ncomms6340. PMID:25500532<ref>PMID:25500532</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 3wo3" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Interleukin|Interleukin]]
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*[[Interleukin receptor|Interleukin receptor]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 09:00, 20 January 2016

Crystal structure of IL-18 in complex with IL-18 receptor alpha

3wo3, resolution 3.10Å

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