Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.
Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.
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哺乳动物细胞外环境中的硫醇-二硫化物交换反应。
DOI：
10.1146/annurev-chembioeng-080615-033553
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发表时间：
2016-06-07
影响因子：
8.4
通讯作者：
Khosla C
中科院分区：
文献类型：
--
作者：
Yi MC;Khosla C
二硫键代表了多功能的翻译后修饰，其作用包括蛋白质的结构、催化和功能调节。由于细胞外环境的氧化性质，分泌蛋白中发现的二硫键曾被认为是惰性的。这一概念受到了氧化还原敏感二硫化物的发现的挑战，一旦切割，可以导致蛋白质活性的变化。这些功能性二硫化物被扭曲成独特的构型，导致高应变和势能。在某些情况下，这些二硫化物的裂解可以导致蛋白质活性功能的获得。因此，这些基序可以被称为开关。我们描述了在细胞外环境中控制氧化还原的电对，研究了具有可切换二硫化物的蛋白质的几个例子，并讨论了二硫化物在分子生物学中的潜在应用。
Disulfide bonds represent versatile posttranslational modifications whose roles encompass the structure, catalysis, and regulation of protein function. Due to the oxidizing nature of the extracellular environment, disulfide bonds found in secreted proteins were once believed to be inert. This notion has been challenged by the discovery of redox-sensitive disulfides that, once cleaved, can lead to changes in protein activity. These functional disulfides are twisted into unique configurations, leading to high strain and potential energy. In some cases, cleavage of these disulfides can lead to a gain of function in protein activity. Thus, these motifs can be referred to as switches. We describe the couples that control redox in the extracellular environment, examine several examples of proteins with switchable disulfides, and discuss the potential applications of disulfides in molecular biology.