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The structure of human interferon-beta: implications for activity.

M Karpusas·A Whitty·L Runkel·P Hochman
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Abstract

Interferons (IFNs) are potent extracellular protein mediators of host defence and homoeostasis. This article reviews the structure of human IFN-beta (HuIFN-beta), in particular in relation to its activity. The recently determined crystal structure of HuIFN-beta provides a framework for understanding of the mechanism of differentiation of type I IFNs by their common receptor. Insights are generated by comparison with the structures of other type I IFNs and from the interpretation of existing mutagenesis data. The details of the observed carbohydrate structure, together with biochemical data, implicate the glycosylation of HuIFN-beta, which is uncommon among type I IFNs, as an important factor in the solubility, stability and, consequently, activity of the protein. Finally, these structural implications are discussed in the context of the clinical use of HuIFN-beta.

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Crystallography, X-RayDimerizationGlycosylationHumansInterferon-betaModels, MolecularProtein BindingProtein Structure, SecondaryReceptors, InterferonJournal ArticleReview

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M Karpusas, A Whitty, L Runkel, P Hochman. 1998. The structure of human interferon-beta: implications for activity.. https://doi.org/10.1007/s000180050248

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