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. 1987 Oct 1;166(4):1055–1069. doi: 10.1084/jem.166.4.1055

The interleukin 2 receptor. Functional consequences of its bimolecular structure

PMCID: PMC2188729  PMID: 3116143

Abstract

High-affinity IL-2-R binding results from an exceptional type of cooperative interaction between two IL-2-binding proteins termed alpha and beta. When expressed together on the cell surface, these two distinct chains form a noncovalent kinetic hybrid receptor complex that exploits a rapid association rate contributed by the p55 beta chain and a slow dissociation rate characteristic for the p75 alpha chain. The p75 alpha chains signal cell growth, whereas the p55 beta chains only facilitate IL-2 binding by serving as helper binding sites, having no discernible signaling role themselves. The unique functional implications of this structural organization indicate that this cooperative bimolecular arrangement reflects a general mechanism by which the efficiency of surface receptors can be enhanced markedly.

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Selected References

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