Bhat, Shashikiran G and Nayek, Upendra and Ajees, Abdul A (2017) In-silico studies on the protein-protein interactions between human Cdc25 and glutaredoxin. Journal of Computational Methods in Sciences and Engineering, 17 (2). pp. 235-242. ISSN 1472-7978

PDF RMS - 2624.pdf - Published Version Restricted to Registered users only Download (2MB) | Request a copy

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.

Actions (login required)

View Item