The structure of human interferon-β:: implications for activity

被引：94

作者：

Karpusas, M ^{[1
]}

Whitty, A ^{[1
]}

Runkel, L ^{[1
]}

Hochman, P ^{[1
]}

机构：

[1] Biogen Inc, Cambridge, MA 02142 USA

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 1998年 / 54卷 / 11期

关键词：

interferon; crystal structure; cytokine; aggregation; glycosylation; multiple sclerosis;

D O I：

10.1007/s000180050248

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1203 / 1216

页数：14

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