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. 1991 Jun 1;88(11):4636–4640. doi: 10.1073/pnas.88.11.4636

Localization in human interleukin 2 of the binding site to the alpha chain (p55) of the interleukin 2 receptor.

K Sauvé 1, M Nachman 1, C Spence 1, P Bailon 1, E Campbell 1, W H Tsien 1, J A Kondas 1, J Hakimi 1, G Ju 1
PMCID: PMC51720  PMID: 2052547

Abstract

Human interleukin 2 (IL-2) analogs with defined amino acid substitutions were used to identify specific residues that interact with the 55-kDa subunit (p55) or alpha chain of the human IL-2 receptor. Analog proteins containing specific substitutions for Lys-35, Arg-38, Phe-42, or Lys-43 were inactive in competitive binding assays for p55. All of these analogs retained substantial competitive binding to the intermediate-affinity p70 subunit (beta chain) of the receptor complex. The analogs varied in ability to interact with the high-affinity p55/p70 receptor. Despite the lack of binding to p55, all analogs exhibited significant biological activity, as assayed on the murine CTLL cell line. The dissociation constants of Arg-38 and Phe-42 analogs for p70 were consistent with intermediate-affinity binding; the Kd values were not significantly affected by the presence of p55 in binding to the high-affinity IL-2 receptor complex. These results confirm the importance of the B alpha-helix in IL-2 as the locus for p55-receptor binding and support a revised model of IL-2-IL-2 receptor interaction.

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Selected References

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