Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 235-242 |
| Number of pages | 8 |
| Journal | Journal of Computational Methods in Sciences and Engineering |
| Volume | 17 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 01-01-2017 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
All Science Journal Classification (ASJC) codes
- General Engineering
- Computer Science Applications
- Computational Mathematics
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