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

Shashikiran G. Bhat, Upendra Nayek, Hiranmoy Bhattacharjee, A. Abdul Ajees

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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 languageEnglish
Pages (from-to)235-242
Number of pages8
JournalJournal of Computational Methods in Sciences and Engineering
Issue number2
Publication statusPublished - 01-01-2017

All Science Journal Classification (ASJC) codes

  • General Engineering
  • Computer Science Applications
  • Computational Mathematics


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