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dc.contributor.authorKrumm, Brian
dc.contributor.authorMeng, Xiangzhi
dc.contributor.authorXiang, Yan
dc.contributor.authorDeng, Junpeng
dc.date.accessioned2018-08-15T12:44:19Z
dc.date.available2018-08-15T12:44:19Z
dc.date.issued2015
dc.identifieroksd_krumm_crystallization_2015
dc.identifier.citationKrumm, B., Meng, X., Xiang, Y., & Deng, J. (2015). Crystallization of interleukin-18 for structure-based inhibitor design. Acta Crystallographica Section F - Structural Biology Communications, 71(6), 710-717. https://doi.org/10.1107/S2053230X15006871
dc.identifier.urihttps://hdl.handle.net/11244/301408
dc.description.abstractInterleukin-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.
dc.formatapplication/pdf
dc.languageen_US
dc.publisherInternational Union of Crystallography
dc.rightsThis material has been previously published. In the Oklahoma State University Library's institutional repository this version is made available through the open access principles and the terms of agreement/consent between the author(s) and the publisher. The permission policy on the use, reproduction or distribution of the material falls under fair use for educational, scholarship, and research purposes. Contact Digital Resources and Discovery Services at lib-dls@okstate.edu or 405-744-9161 for further information.
dc.titleCrystallization of interleukin-18 for structure-based inhibitor design
osu.filenameoksd_krumm_crystallization_2015.pdf
dc.description.peerreviewPeer reviewed
dc.identifier.doi10.1107/S2053230X15006871
dc.description.departmentBiochemistry and Molecular Biology
dc.type.genreArticle
dc.type.materialText
dc.subject.keywordscytokines
dc.subject.keywordsimmune defense
dc.subject.keywordsinterleukin-18
dc.subject.keywordssurface-entropy reduction


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