[Function, molecular structure and gene expression of IL-2 and the receptors].
The Interleukin 2 receptor is now assumed to be composed of three chains, the L (alpha or Tac), H (beta) chain and p56. The L chain binds IL-2 with low affinity, whereas intermediate-affinity binding of IL-2 is achieved by an association of p56 and the H chain. The high-affinity IL-2R is therefore believed to be a quaternary complex composed of the L chain, the H chain, p56 and IL-2. A larger number of L chains enhances the association rate of IL-2 to form the high-affinity IL-2R in agreement with the stepwise binding model. The signal transduction-competent H chain has been shown to associate with p56lck upon IL-2 stimulation.
Saito
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Department of Medical Chemistry, Faculty of Medicine, Kyoto University.
D000818:Animals; D006801:Humans; D007376:Interleukin-2 / Q000502:physiology*; D015375:Receptors, Interleukin-2 / Q000502:physiology*
D007376:Interleukin-2; D015375:Receptors, Interleukin-2