Abstract
The Type I interferons (IFN-α / ß) exhibit pleiotropic biological activities. Notably, the different IFN subtypes activate the same cell surface receptor complex to mediate variable responses. Accumulating evidence suggests that distinct differences in critical amino acid residues among the different IFN-αs and IFN-ß determine the nature of the ligand-receptor interaction and the subsequent responses. This review focuses on IFN-receptor interactions, the key residues involved in this interaction and the potential for targeted modifications of the ligand to enhance bioactivity.
Keywords: interferon, ifnar1, ifnar2, binding residues
Current Pharmaceutical Design
Title: Interferon-α / β-Receptor Interactions: A Complex Story Unfolding
Volume: 8 Issue: 24
Author(s): Raj Deonarain, David C.M. Chan, Leonidas C. Platanias and Eleanor N. Fish
Affiliation:
Keywords: interferon, ifnar1, ifnar2, binding residues
Abstract: The Type I interferons (IFN-α / ß) exhibit pleiotropic biological activities. Notably, the different IFN subtypes activate the same cell surface receptor complex to mediate variable responses. Accumulating evidence suggests that distinct differences in critical amino acid residues among the different IFN-αs and IFN-ß determine the nature of the ligand-receptor interaction and the subsequent responses. This review focuses on IFN-receptor interactions, the key residues involved in this interaction and the potential for targeted modifications of the ligand to enhance bioactivity.
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Cite this article as:
Deonarain Raj, Chan C.M. David, Platanias C. Leonidas and Fish N. Eleanor, Interferon-α / β-Receptor Interactions: A Complex Story Unfolding, Current Pharmaceutical Design 2002; 8 (24) . https://dx.doi.org/10.2174/1381612023393288
DOI https://dx.doi.org/10.2174/1381612023393288 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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