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In-silico studies on the protein-protein interactions between human Cdc25 and glutaredoxin

机译:在计算机上研究人Cdc25与戊二醛之间的蛋白质相互作用

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Arsenic is a hazardous substance and exposure to inorganic arsenic leads to various vascular and carcinogenic diseases. Reduction of pentavalent arsenical to trivalency plays a critical role in its detoxification. We have earlier shown that human Cdc25B or Cdc25C protein tyrosine phosphatase catalyzes the reduction of inorganic arsenate to arsenite. Human glutaredoxin-1 functions as a hydrogen donor for Cdc25 catalyzed arsenate reduction. In this paper, molecular docking studies were performed to understand the interactions between Cdc25 and the two dicysteinic glutaredoxins, glutaredoxin-1 and glutaredoxin-2, and the monothiol glutaredoxin-3.
机译:砷是一种有害物质,接触无机砷会导致各种血管和致癌性疾病。五价砷还原为三价化合物在其排毒中起关键作用。我们之前已经表明,人类Cdc25B或Cdc25C蛋白酪氨酸磷酸酶催化将无机砷酸盐还原为亚砷酸盐。人glutaredoxin-1充当氢供体,用于Cdc25催化的砷酸盐还原。在本文中,进行了分子对接研究,以了解Cdc25与两种半胱氨酸谷胱甘肽毒素glutaredoxin-1和glutaredoxin-2和一硫醇glutaredoxin-3之间的相互作用。

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