TY - JOUR
T1 - In-silico studies on the protein-protein interactions between human Cdc25 and glutaredoxin
AU - Bhat, Shashikiran G.
AU - Nayek, Upendra
AU - Bhattacharjee, Hiranmoy
AU - Ajees, A. Abdul
N1 - Publisher Copyright:
© 2017 IOS Press and the authors. All rights reserved.
PY - 2017/1/1
Y1 - 2017/1/1
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/85018373812
UR - https://www.scopus.com/pages/publications/85018373812#tab=citedBy
U2 - 10.3233/JCM-170717
DO - 10.3233/JCM-170717
M3 - Article
AN - SCOPUS:85018373812
SN - 1472-7978
VL - 17
SP - 235
EP - 242
JO - Journal of Computational Methods in Sciences and Engineering
JF - Journal of Computational Methods in Sciences and Engineering
IS - 2
ER -
