ArticleProceedings of the National Academy of Sciences of the United States of America1995
Mutagenesis in the C-terminal region of human interleukin 5 reveals a central patch for receptor alpha chain recognition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 38 citations in OpenAlex.
- Utilization of extracellular information before ligand-receptor binding reaches equilibrium expands and shifts the input dynamic range.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural basis of interleukin-5 dimer recognition by its α receptor.Protein science : a publication of the Protein Society · 2012Article
- Asymmetric usage of antagonist charged residues drives interleukin-5 receptor recruitment but is insufficient for receptor activation.Biochemistry · 2006Article
- Expression and in vitro properties of guinea pig IL-5: comparison to human and murine orthologs.Mediators of inflammation · 2000Article
- Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonance.Journal of virology · 1998Article
- Monomeric isomers of human interleukin 5 show that 1:1 receptor recruitment is sufficient for function.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Engineering of a functional interleukin-5 monomer: a paradigm for redesigning helical bundle cytokines with therapeutic potential in allergy and asthma.Journal of molecular medicine (Berlin, Germany) · 1996Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Cassette mutagenesis was used to identify side chains in human interleukin 5 (hIL-5) that mediate binding to hIL-5 receptor alpha chain (hIL-5R alpha). A series of single alanine substitutions was introduced into a stretch of residues in the C-terminal region, including helix D, which previously had been implicated in receptor alpha chain recognition and which is aligned on the IL-5 surface so as to allow the topography of receptor binding residues to be examined. hIL-5 and single site mutants were expressed in COS cells, their interactions with hIL-5R alpha were measured by a sandwich surface plasmon resonance biosensor method, and their biological activities were measured by an IL-5-dependent cell proliferation assay. A pattern of mutagenesis effects was observed, with greatest impact near the interface between the two four-helix bundles of IL-5, in particular at residues Glu-110 and Trp-111, and least at the distal ends of the D helices. This pattern suggests the possibility that residues near the interface of the two four-helix bundles in hIL-5 comprise a central patch or hot spot, which constitutes an energetically important alpha chain recognition site. This hypothesis suggests a structural explanation for the 1:1 stoichiometry observed for the complex of hIL-5 with hIL-5R alpha.
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