Structural and functional aspects of C1-Inhibitor

被引：49

作者：

Bos, IGA

Hack, CE

Abrahams, JP

机构：

[1] CLB, Dept Immunopathol, Sanquin Res, NL-1066 CX Amsterdam, Netherlands

[2] Univ Amsterdam, Acad Med Ctr, Landsteiner Lab, NL-1105 AZ Amsterdam, Netherlands

[3] Vrije Univ Amsterdam, Med Ctr, Dept Clin Chem, Amsterdam, Netherlands

[4] Leiden Inst Chem, Leiden, Netherlands

来源：

IMMUNOBIOLOGY | 2002年 / 205卷 / 4-5期

关键词：

D O I：

10.1078/0171-2985-00151

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

C1-Inh is a serpin that inhibits serine proteases from the complement and the coagulation pathway. C1-Inh consists of a serpin domain and a unique N-terminal domain and is heavily glycosylated. Nonfunctional mutants of C1-Inh can give insight into the inhibitory mechanism of C1-Inh. This review describes a novel 3D model of C1-Inh, based on a newly developed homology modelling method. This model gives insight into a possible potentiation mechanism of C1-Inh and based on this model the essential residues for efficient inhibition by C1-Inh are discussed.

引用

收藏

页码：518 / 533

页数：16

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