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Identification of Key Charged Residues of Human Interleukin-5 in Receptor Binding and Cellular Activation (*)
TLDR
The α-chain binding site is shown to involve the side chains Arg-90 and Glu-109, located in the second β sheet and after the end of the fourth helix, respectively, which is unique to IL-5 and does not occur in IL-3 or GM-CSF.
An Interleukin 5 Mutant Distinguishes between Two Functional Responses in Human Eosinophils
TLDR
ThisIL-5 mutant enables us to clearly distinguish between two IL-5–dependent functional responses and reveals distinct mechanisms of receptor/cellular activation.
Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity in mouse uterine epithelial cells.
TLDR
It is concluded that, although all components for a reversible phosphorylative regulation of 3-hydroxy-3-methylglutaryl-CoA reductase activity are present in uterine epithelial cells, a role in the rapid changes in epithelial enzyme activity has not been demonstrated.
Soluble interleukin-5 receptor alpha-chain binding assays: use for screening and analysis of interleukin-5 mutants.
TLDR
Two receptor/ligand binding assays based on the extracellular domain of the receptor alpha-chain are established and three assays used to study site-directed mutants of IL-5 to determine the important residues for interaction of the cytokine with each chain of the receptors are established.
The carboxy-terminal region of human interleukin-5 is essential for maintenance of tertiary structure but not for dimerization
TLDR
The C-terminal region of interleukin-5 has previously been suggested to be important for biological activity and is investigated by making a series of truncation mutants, which showed a rapid loss of activity and a drop in binding affinity to both theα chain of the receptor and the high-affinity complex consisting of theα andβ subunits.
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