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==Crystal structure of the IL-18 signaling ternary complex== | ==Crystal structure of the IL-18 signaling ternary complex== | ||
<StructureSection load='3wo4' size='340' side='right' caption='[[3wo4]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='3wo4' size='340' side='right'caption='[[3wo4]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wo4]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WO4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3wo4]] is a 3 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=3WO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WO4 FirstGlance]. <br> | ||
</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wo4 OCA], [https://pdbe.org/3wo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wo4 RCSB], [https://www.ebi.ac.uk/pdbsum/3wo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wo4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wo4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Interleukin 3D structures|Interleukin 3D structures]] | |||
*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arita | [[Category: Homo sapiens]] | ||
[[Category: Ariyoshi | [[Category: Large Structures]] | ||
[[Category: Kato | [[Category: Arita K]] | ||
[[Category: Kimura | [[Category: Ariyoshi M]] | ||
[[Category: Kondo | [[Category: Kato Z]] | ||
[[Category: Ohnishi | [[Category: Kimura T]] | ||
[[Category: Shirakawa | [[Category: Kondo N]] | ||
[[Category: Tochio | [[Category: Ohnishi H]] | ||
[[Category: Tsutsumi | [[Category: Shirakawa M]] | ||
[[Category: Tochio H]] | |||
[[Category: Tsutsumi N]] | |||
Latest revision as of 16:18, 8 November 2023
Crystal structure of the IL-18 signaling ternary complexCrystal structure of the IL-18 signaling ternary complex
Structural highlights
FunctionIL18_HUMAN Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. Publication Abstract from PubMedInterleukin (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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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