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• W2032082763 abstract "Human interleukin-11 (hIL-11) is a pleiotropic cytokine administered to patients with low platelet counts. From a structural point of view hIL-11 belongs to the long-helix cytokine superfamily, which is characterized by a conserved core motif consisting of four α-helices. We have investigated the region of hIL-11 that does not belong to the α-helical bundle motif, and that for the purpose of brevity we have termed non-core region. The primary sequence of the interleukin was altered at various locations within the non-core region by introducing glycosylation sites. Functional consequences of these modifications were examined in cell-based as well as biophysical assays. Overall, the data indicated that the non-core region modulates the function of hIL-11 in two ways. First, the majority of muteins displayed enhanced cell-stimulatory properties (superagonist behavior) in a glycosylation-dependent manner, suggesting that the non-core region is biologically designed to limit the full potential of hIL-11. Second, specific modification of a predicted mini α-helix led to cytokine inactivation, demonstrating that this putative structural element belongs to site III engaging a second copy of cell-receptor gp130. These findings have unveiled new and unexpected elements modulating the biological activity of hIL-11, which may be exploited to develop more versatile medications based on this important cytokine." @default.
• W2032082763 created "2016-06-24" @default.
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• W2032082763 date "2011-03-01" @default.
• W2032082763 modified "2023-10-12" @default.
• W2032082763 title "Non-core Region Modulates Interleukin-11 Signaling Activity" @default.
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• W2032082763 doi "https://doi.org/10.1074/jbc.m110.152561" @default.
• W2032082763 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3048695" @default.
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