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• W115589848 abstract "Research Article1 November 1992free access Receptor antagonist and selective agonist derivatives of mouse interleukin-2. S.M. Zurawski S.M. Zurawski Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104. Search for more papers by this author G. Zurawski G. Zurawski Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104. Search for more papers by this author S.M. Zurawski S.M. Zurawski Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104. Search for more papers by this author G. Zurawski G. Zurawski Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104. Search for more papers by this author Author Information S.M. Zurawski1 and G. Zurawski1 1Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104. The EMBO Journal (1992)11:3905-3910https://doi.org/10.1002/j.1460-2075.1992.tb05483.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Mouse interleukin-2 (mIL-2) proteins with substitutions at two residues (D34 and Q141) that interact specifically with different signalling subunits (respectively, beta and gamma) of the IL-2 receptor (IL-2R) were examined using several in vitro cellular assays. Proteins with specific substitutions at both residues were partial agonists and their maximal responses varied widely in different IL-2-responsive cell types. Two of these cell types had comparable numbers of IL-2R and similar affinities for wild-type mIL-2 and mutant mIL-2 proteins. However, the more responsive cell type had ‘spare’ IL-2R. Various mIL-2 proteins with substitutions at Q141 had modest defects in IL-2R-binding and were potent antagonists of native mIL-2 action. Proteins with bulky or basic substitutions at residue D34 were weak antagonists due to severely reduced IL-2 binding and their reduced binding paralleled their defects in IL-2R activation. Our results suggest that interaction of mIL-2 with IL-2R beta is more important for binding than activation and that the converse holds for mIL-2 interaction with IL-2R gamma. Also genetic manipulation of the interaction of IL-2 with IL-2R beta and IL-2R gamma has led to the discovery of potentially useful IL-2 antagonists and selective agonists. Previous ArticleNext Article Volume 11Issue 111 November 1992In this issue RelatedDetailsLoading ..." @default.
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• W115589848 title "Receptor antagonist and selective agonist derivatives of mouse interleukin-2." @default.
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