Determination of the minimum polypeptide lengths of the functionally active sites of human interleukins 1 alpha and 1 beta.

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Abstract
Interleukin 1 (IL-1) is a two-member family of proteins (IL-1.alpha. and IL-1.beta.) that mediates a diverse series of immune and inflammatory responses. These two proteins have only 26% amino acid homology yet bind to the same receptor. It is of importance to define the active sites of these molecules in order to understand their receptor interactions and the mechanisms involved in their multiple biological functions. We report here the localization of the biologically active portions within the initial polypeptide translation products. An in vitro transcription and translation system was used to generate specific fragments of each of the IL-1 molecules, which then were assayed for receptor binding capability and biological activity. Using the system, we have demonstrated that core sequences of 147 amino acids for IL-1.beta. (numbers 120-266) and 140 amino acids for IL-1.alpha. (numbers 128-267) must be left intact to retain full biological activity and further that the biological activities of the IL-1 polypeptides parallel their receptor binding capabilities.