Title

Authors

Affiliation

¹Department of Experimental Medicine and Biotechnology, Postgraduate Institute of Medical Education and Research (PGIMER), Chandigarh-160012, India; ²Synthetic Biology and Biofuel Group; International Centre for Genetic Engineering and Biotechnology (ICGEB); New Delhi-110067, India; ³S P. Institute of Biotechnology (Training and Research), E-734-735, Nakul Path, Lal Kothi Scheme, Jaipur, Rajasthan-302015, India.

Email

hemant@icgeb.res.in; *Corresponding authors

Article Type

Hypothesis

Date

Received January 07, 2013; Accepted January 11, 2013; Published March 02, 2013

Glutaredoxins are enzymatic antioxidants which are small, ubiquitous, glutathione dependent and essentially classified under thioredoxin-fold superfamily. Glutaredoxins are classified into two types: dithiol and monothiol. Monothiol glutaredoxins which carry the signature “CGFS” as a redox active motif is known for its role in oxidative stress, inside the cell. In the present analysis, the 138 amino acid long monothiol glutaredoxin, AgGRX1 from Ashbya gossypii was identified and has been used for the analysis. The multiple sequence alignment of the AgGRX1 protein sequence revealed the characteristic motif of typical monothiol glutaredoxin as observed in various other organisms. The proposed structure of the AgGRX1 protein was used to analyze signature folds related to the thioredoxin superfamily. Further, the study highlighted the structural features pertaining to the complex mechanism of glutathione docking and interacting residues.

Keywords

Ashbya, GRX, Monothiol, glutaredoxin, Homology modelling, Docking.

Citation

Yadav  et al.   Bioinformation 9(5): 243-249 (2013)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.