Hogg P J
UNSW Cancer Research Centre, University of New South Wales, Sydney, NSW, Australia.
J Thromb Haemost. 2009 Jul;7 Suppl 1:13-6. doi: 10.1111/j.1538-7836.2009.03364.x.
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.
蛋白质二硫键是多肽链中半胱氨酸残基对之间的共价连接。二硫键的获得是蛋白质进化并仍在持续进化的重要方式。这些键发挥结构或功能作用。有两种功能性二硫键：存在于氧化还原酶活性位点的催化键和变构键。变构二硫键被定义为通过以精确方式断裂或形成来控制蛋白质功能方式而进化形成的键。已知的变构键具有一种称为-RHStaple的特定构型。几种止血蛋白含有-RHStaple二硫键，并且越来越多的证据表明其中一些键可能参与其所存在蛋白质的功能。迄今为止对此研究最深入的是组织因子中的-RHStaple二硫键及其在辅因子解密中的作用。
