4r6u: Difference between revisions
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==IL-18 receptor complex== | |||
<StructureSection load='4r6u' size='340' side='right'caption='[[4r6u]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4r6u]] is a 4 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=4R6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R6U FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=4r6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r6u OCA], [https://pdbe.org/4r6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r6u RCSB], [https://www.ebi.ac.uk/pdbsum/4r6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r6u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses. It signals through its ligand-binding primary receptor IL-18Ralpha and accessory receptor IL-18Rbeta. Here we report the crystal structure of IL-18 with the ectodomain of IL-18Ralpha, which reveals the structural basis for their specific recognition. It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family. We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family. | |||
Structural basis for the specific recognition of IL-18 by its alpha receptor.,Wei H, Wang D, Qian Y, Liu X, Fan S, Yin HS, Wang X FEBS Lett. 2014 Sep 26. pii: S0014-5793(14)00696-6. doi:, 10.1016/j.febslet.2014.09.019. PMID:25261253<ref>PMID:25261253</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4r6u" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Interleukin 3D structures|Interleukin 3D structures]] | |||
*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Wang X]] | |||
[[Category: Wei H]] | |||
