| Literature DB >> 9849615 |
M Karpusas1, A Whitty, L Runkel, P Hochman.
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.Entities:
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Year: 1998 PMID： 9849615 DOI： 10.1007/s000180050248
Source DB: PubMed Journal: Cell Mol Life Sci ISSN： 1420-682X Impact factor: 9.261