title: The structure of human interferon-beta: implications for activity.
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.
authors.affiliation: Biogen Inc., 14 Cambridge Center, Cambridge, Massachusetts 02142, USA. michael_karpusas@biogen.com
authors.forename: M
authors.initials: M
authors.lastname: Karpusas
authors.forename: A
authors.initials: A
authors.lastname: Whitty
authors.forename: L
authors.initials: L
authors.lastname: Runkel
authors.forename: P
authors.initials: P
authors.lastname: Hochman
mesh_terms: D018360:Crystallography, X-Ray; D019281:Dimerization; D006031:Glycosylation; D006801:Humans; D016899:Interferon-beta / Q000737:chemistry* / Q000627:therapeutic use; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017471:Receptors, Interferon / Q000737:chemistry
chemical_list: D017471:Receptors, Interferon; D016899:Interferon-beta