4xfu

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m (Protected "4xfu" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 4xfu is ON HOLD
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==Structure of IL-18 SER Mutant V==
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<StructureSection load='4xfu' size='340' side='right'caption='[[4xfu]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xfu]] 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=4XFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XFU 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]] 2.85&#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=4xfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xfu OCA], [https://pdbe.org/4xfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xfu RCSB], [https://www.ebi.ac.uk/pdbsum/4xfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xfu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interleukin-18 (IL-18) is a pleiotropic pro-inflammatory cytokine belonging to the IL-1 superfamily. IL-18 plays an important role in host innate and acquired immune defense, with its activity being modulated in vivo by its naturally occurring antagonist IL-18 binding protein (IL-18BP). Recent crystal structures of human IL-18 (hIL-18) in complex with its antagonist or cognate receptor(s) have revealed a conserved binding interface on hIL-18 representing a promising drug target. An important step in this process is obtaining crystals of apo hIL-18 or hIL-18 in complex with small-molecule inhibitors, preferably under low ionic strength conditions. In this study, surface-entropy reduction (SER) and rational protein design were employed to facilitate the crystallization of hIL-18. The results provide an excellent platform for structure-based drug design.
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Authors: Krumm, B.E., Meng, X., Xiang, Y., Deng, J.
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Crystallization of interleukin-18 for structure-based inhibitor design.,Krumm B, Meng X, Xiang Y, Deng J Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):710-7. doi:, 10.1107/S2053230X15006871. Epub 2015 May 20. PMID:26057800<ref>PMID:26057800</ref>
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Description: Structure of IL-18 SER Mut V
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Deng, J]]
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<div class="pdbe-citations 4xfu" style="background-color:#fffaf0;"></div>
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[[Category: Krumm, B.E]]
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[[Category: Meng, X]]
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==See Also==
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[[Category: Xiang, Y]]
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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: Deng J]]
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[[Category: Krumm BE]]
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[[Category: Meng X]]
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[[Category: Xiang Y]]

Current revision

Structure of IL-18 SER Mutant V

PDB ID 4xfu

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