4xfs

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== Function ==
== Function ==
[[http://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.
[[http://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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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 12:12, 1 July 2015

Structure of IL-18 SER Mutant I

4xfs, resolution 1.91Å

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