8urv: Difference between revisions

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-'''Unreleased structure'''
-The entry 8urv is ON HOLD
+==Solution NMR structure of pro-IL-18==
+<StructureSection load='8urv' size='340' side='right'caption='[[8urv]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8urv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8URV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8URV FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8urv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8urv OCA], [https://pdbe.org/8urv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8urv RCSB], [https://www.ebi.ac.uk/pdbsum/8urv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8urv ProSAT]</span></td></tr>
+</table>
+== 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 ==
+Several interleukin-1 (IL-1) family members, including IL-1beta and IL-18, require processing by inflammasome-associated caspases to unleash their activities. Here, we unveil, by cryoelectron microscopy (cryo-EM), two major conformations of the complex between caspase-1 and pro-IL-18. One conformation is similar to the complex of caspase-4 and pro-IL-18, with interactions at both the active site and an exosite (closed conformation), and the other only contains interactions at the active site (open conformation). Thus, pro-IL-18 recruitment and processing by caspase-1 is less dependent on the exosite than the active site, unlike caspase-4. Structure determination by nuclear magnetic resonance uncovers a compact fold of apo pro-IL-18, which is similar to caspase-1-bound pro-IL-18 but distinct from cleaved IL-18. Binding sites for IL-18 receptor and IL-18 binding protein are only formed upon conformational changes after pro-IL-18 cleavage. These studies show how pro-IL-18 is selected as a caspase-1 substrate, and why cleavage is necessary for its inflammatory activity.
-Authors:
+Structural transitions enable interleukin-18 maturation and signaling.,Dong Y, Bonin JP, Devant P, Liang Z, Sever AIM, Mintseris J, Aramini JM, Du G, Gygi SP, Kagan JC, Kay LE, Wu H Immunity. 2024 May 8:S1074-7613(24)00220-6. doi: 10.1016/j.immuni.2024.04.015. PMID:38733997<ref>PMID:38733997</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8urv" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Aramini JM]]
+[[Category: Bonin JP]]
+[[Category: Kay LE]]