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Eur J Biochem. 1995 Mar 1;228(2):305-10.

An antagonistic mutant of interleukin-4 fails to recruit gamma c into the receptor complex. Characterization by specific crosslinking.

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Theodor-Boveri-Institute für Biowissenschaften, Würzburg, Germany.


The receptor for interleukin-4 (IL-4) appears to be a heterodimer of the IL-4-binding protein IL-4R alpha and the gamma c chain. Mutations of IL-4 have previously identified a region of IL-4 essential for signaling, which was suggested to bind gamma c. Here it is shown by crosslinking of radiolabeled ligand and precipitation with specific antibodies that mutations in the IL-4 signaling site prevent association of gamma c, but not binding to IL-4R alpha. This demonstrates that an intact signaling site of IL-4 is required to recruit gamma c into the receptor complex, while specific mutants are antagonists because they fail to achieve this.

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