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In this report, we have investigated the kinetics of IL-2 binding to the alpha (p55) and beta (p70) IL-2 binding proteins and compared these properties with ligand binding to the high-affinity IL-2-R. The association and dissociation of IL-2 to the alpha (p55) chain occurred with very rapid kinetics (t 1/2 = 4-10 s). In contrast, IL-2 association to, and dissociation from the beta (p70) chain occurred at a greatly reduced rate (t 1/2 = 40-50 min and 200-400 min, respectively). Measurements of IL-2 binding to the high-affinity receptor revealed an interesting composite of these binding properties with a rapid association rate (t 1/2 = 30-45 s) resembling the alpha (p55) chain and a slow dissociation rate (t 1/2 = 270-300 min) similar to the beta (p70) chain. These findings provide additional support for the model of the high-affinity IL-2-R as a heterodimeric membrane complex composed of both the alpha (p55) and beta (p70) subunits and suggest that high-affinity IL-2 binding may involve a conformational change in structure of either or possibly both of the receptor chains. These results highlight the important and perhaps different role played by each subunit in the formation of functional high-affinity IL-2-R.

Contrasting interleukin 2 binding properties of the alpha (p55) and beta (p70) protein subunits of the human high-affinity interleukin 2 receptor.