Title

Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi

Authors

Rayavarapu Bhargavi¹, Siddharth Vishwakarma² and Upadhyayula Suryanarayana Murty*¹

Affiliation

¹Bioinformatics Group, Biology Division, Indian Institute of Chemical Technology, Hyderabad, India; ²Department of P.G. Studies & Research in Biological science, RDVV, Jabalpur, India

E-mail*

murty_usn@yahoo.com; * Corresponding author

Article Type

Hypothesis

Date

received April 20, 2005; accepted  May 5, 2005; published online June 2, 2005

Abstract

GST (glutathione S-transferases) are a family of detoxification enzymes that catalyze the conjugation of reduced GSH (glutathione) to xenobiotic (endogenous electrophilic) compounds. GST from Wb (Wuchereria bancrofti) and Bm (Brugia malayi) are significantly different from human GST in sequence and structure. Thus, Wb-GST and Bm-GST are potential chemotherapeutic targets for anti-filarial treatment. Comparison of modeled Wb and Bm GST with human GST show structural difference between them. Analysis of the active site residues for the binding of electrophilic co-substrates provides insight towards the design of parasite specific GST inhibitors.

Keywords

Filarial parasites; GST (glutathione-S-transferases); homology modeling; structural deviations; active site residues

Citation

Bhargavi et al., Bioinformation 1(1): 25-27 (2005)

Edited by

V. S. Mathura

ISSN

0973-2063

Publisher

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.