Disulfide bonds as switches for protein function

被引：515

作者：

Hogg, PJ ^{[1
]}

机构：

[1] Univ New S Wales, Ctr Vasc Res, Sydney, NSW 2052, Australia

[2] Prince Wales Hosp, Dept Haematol, Sydney, NSW 2052, Australia

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2003年 / 28卷 / 04期

基金：

英国医学研究理事会; 澳大利亚研究理事会;

关键词：

D O I：

10.1016/S0968-0004(03)00057-4

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：

The prevailing view is that disulfide bonds have been added during evolution to enhance the stability of proteins that function in a fluctuating cellular environment. However, recent evidence indicates that disulfide bonds can be more than inert structural motifs. The function of some secreted soluble proteins and cell-surface receptors is controlled by cleavage of one or more of their disulfide bonds; this cleavage is mediated by catalysts or facilitators that are specific for their substrate.

引用

页码：210 / 214

页数：5

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