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. 1991 Dec;10(13):4105–4112. doi: 10.1002/j.1460-2075.1991.tb04987.x

The amino-terminal helix of GM-CSF and IL-5 governs high affinity binding to their receptors.

A B Shanafelt 1, A Miyajima 1, T Kitamura 1, R A Kastelein 1
PMCID: PMC453160  PMID: 1836758

Abstract

Transduction of the biological effects of granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin-5 (IL-5) requires the interaction of each cytokine with at least two cell surface receptor components, one of which is shared between these two cytokines. A strategy is presented that allowed us to identify receptor binding determinants in GM-CSF and IL-5. Mixed species (human and mouse) receptors were used to locate unique receptor binding domains on a series of human-mouse hybrid GM-CSF and IL-5 cytokines. Results show that the interaction of these two cytokines with the shared subunit of their high affinity receptor complexes is governed by a very small part of their peptide chains. The presence of a few key residues in the amino-terminal alpha-helix of each ligand is sufficient to confer specificity to the interaction. Comparison with other cytokines suggests that the amino-terminal helix of many of these proteins may contain the recognition element for the formation of high affinity binding sites with the alpha subunit of their multi-component receptors.

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Selected References

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