4xfu: Difference between revisions
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==Structure of IL-18 SER Mutant V== | ==Structure of IL-18 SER Mutant V== | ||
<StructureSection load='4xfu' size='340' side='right' caption='[[4xfu]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='4xfu' size='340' side='right'caption='[[4xfu]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xfu]] is a 2 chain structure. 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 [ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</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=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> | ||
</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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4xfu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4xfu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Interleukin 3D structures|Interleukin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Deng J]] | ||
[[Category: | [[Category: Krumm BE]] | ||
[[Category: | [[Category: Meng X]] | ||
[[Category: | [[Category: Xiang Y]] | ||
Latest revision as of 10:45, 27 September 2023
Structure of IL-18 SER Mutant VStructure of IL-18 SER Mutant V
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-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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