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 with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XFU FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xfu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XFU FirstGlance]. <br> | ||
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</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/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Deng, J]] | [[Category: Deng, J]] | ||
[[Category: Krumm, B E]] | [[Category: Krumm, B E]] | ||
Revision as of 18:48, 11 December 2019
Structure of IL-18 SER Mutant VStructure of IL-18 SER Mutant V
Structural highlights
Function[IL18_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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