ArticleProtein science : a publication of the Protein Society1999
Characterization of a soluble ternary complex formed between human interferon-beta-1a and its receptor chains.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Apolipoprotein D downregulation in OSCC: multi-database validation and clinical significance.BMC medical genomics · 2026Article
- Efficient mutagenesis targeting theAmerican journal of translational research · 2021Article
- Review
- Ligand-independent interaction of the type I interferon receptor complex is necessary to observe its biological activity.Cytokine · 2013Article
- Conformation and dynamics of biopharmaceuticals: transition of mass spectrometry-based tools from academe to industry.Journal of the American Society for Mass Spectrometry · 2010Article
- Detection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches.Analytical chemistry · 2008Article
- Antiviral activities of the soluble extracellular domains of type I interferon receptors.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Jak-Stat signal transduction pathway through the eyes of cytokine class II receptor complexes.Oncogene · 2000Review
- Understanding cytokine and growth factor receptor activation mechanisms.Critical reviews in biochemistry and molecular biologyReview
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10 authors.
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Abstract
The extracellular portions of the chains that comprise the human type I interferon receptor, IFNAR1 and IFNAR2, have been expressed and purified as recombinant soluble His-tagged proteins, and their interactions with each other and with human interferon-beta-1a (IFN-beta-1a) were studied by gel filtration and by cross-linking. By gel filtration, no stable binary complexes between IFN-beta-1a and IFNAR1, or between IFNAR1 and IFNAR2 were detected. However, a stable binary complex formed between IFN-beta-1a and IFNAR2. Analysis of binary complex formation using various molar excesses of IFN-beta-1a and IFNAR2 indicated that the complex had a 1:1 stoichiometry, and reducing SDS-PAGE of the binary complex treated with the cross-linking reagent dissucinimidyl glutarate (DSG) indicated that the major cross-linked species had an apparent Mr consistent with the sum of its two individual components. Gel filtration of a mixture of IFNAR1 and the IFN-beta-1a/IFNAR2 complex indicated that the three proteins formed a stable ternary complex. Analysis of ternary complex formation using various molar excesses of IFNAR1 and the IFN-beta-1a/IFNAR2 complex indicated that the ternary complex had a 1:1:1 stoichiometry, and reducing SDS-PAGE of the ternary complex treated with DSG indicated that the major cross-linked species had an apparent Mr consistent with the sum of its three individual components. We conclude that the ternary complex forms by the sequential association of IFN-beta-1a with IFNAR2, followed by the association of IFNAR1 with the preformed binary complex. The ability to produce the IFN-beta-1a/IFNAR2 and IFN-beta-1a/IFNAR1/IFNAR2 complexes make them attractive candidates for X-ray crystallography studies aimed at determining the molecular interactions between IFN-beta-1a and its receptor.
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