Contribution of allosteric disulfide bonds to regulation of hemostasis
Contribution of allosteric disulfide bonds to regulation of hemostasis
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DOI：
10.1111/j.1538-7836.2009.03364.x
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发表时间：
2009-07-01
影响因子：
10.4
通讯作者：
Hogg, P. J.
中科院分区：
文献类型：
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作者：
Hogg, P. J.
蛋白质二硫键是多肽链上两对半胱氨酸残基之间的共价键。二硫键的获得是蛋白质进化的一种重要方式，并且还在继续进化。这些纽带既有结构性作用，也有功能性作用。有两种类型的功能二硫键：位于氧化还原酶活性中心的催化键和变构键。变构二硫化物被定义为通过以精确的方式断裂或形成来控制蛋白质功能的键。已知的变构键有一种特殊的构型，称为-RHStaple。一些止血蛋白含有-RHStaple二硫化物，越来越多的证据表明，其中一些键可能与它们所在的蛋白质的功能有关。到目前为止，研究得最好的是组织因子中的-RHStaple二硫化物及其在辅因子解密中的作用。
Protein disulfide bonds are covalent links between pairs of Cys residues in the polypeptide chain. Acquisition of disulfide bonds is an important way that proteins have evolved and are continuing to evolve. These bonds serve either a structural or functional role. There are two types of functional disulfide: the catalytic bonds that reside in the active sites of oxidoreductases and the allosteric bonds. Allosteric disulfides are defined as bonds that have evolved to control the manner in which proteins function by breaking or forming in a precise way. The known allosteric bonds have a particular configuration known as the -RHStaple. Several hemostasis proteins contain -RHStaple disulfides and there is increasing evidence that some of these bonds may be involved in the functioning of the protein in which they reside. The best studied of these to date is the -RHStaple disulfide in tissue factor and its role in de-encryption of the cofactor.