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

Issue title: Selected Papers from ICCMEH2014

Guest editors: Raghuvir Pai

Article type: Research Article

Authors: Bhat, Shashikiran G.^a | Nayek, Upendra^a | Bhattacharjee, Hiranmoy^b | Abdul Ajees, A.^{a; *}

Affiliations: [a] Department of Atomic and Molecular Physics, Manipal University, Manipal, Karnataka 576104, India | [b] Department of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami 33199, FL, USA

Correspondence: [*] Corresponding author: A. Abdul Ajees, Department of Atomic and Molecular Physics, Manipal University, Manipal, Karnataka 576104, India. E-mail:[email protected]

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.

Keywords: Arsenic, Cdc25, docking, Glrx

DOI: 10.3233/JCM-170717

Journal: Journal of Computational Methods in Sciences and Engineering, vol. 17, no. 2, pp. 235-242, 2017