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.
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