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

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 huma...

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Main Authors:	Bhargavi, Rayavarapu, Vishwakarma, Siddharth, Murty, Upadhyayula Suryanarayana
Format:	Online
Language:	English
Published:	Biomedical Informatics Publishing Group 2005
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891627/

id	pubmed-1891627
recordtype	oai_dc
spelling	pubmed-18916272007-06-27 Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi Bhargavi, Rayavarapu Vishwakarma, Siddharth Murty, Upadhyayula Suryanarayana Hypothesis 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. Biomedical Informatics Publishing Group 2005-06-02 /pmc/articles/PMC1891627/ /pubmed/17597848 Text en © 2005 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Bhargavi, Rayavarapu Vishwakarma, Siddharth Murty, Upadhyayula Suryanarayana
spellingShingle	Bhargavi, Rayavarapu Vishwakarma, Siddharth Murty, Upadhyayula Suryanarayana Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi
author_facet	Bhargavi, Rayavarapu Vishwakarma, Siddharth Murty, Upadhyayula Suryanarayana
author_sort	Bhargavi, Rayavarapu
title	Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi
title_short	Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi
title_full	Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi
title_fullStr	Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi
title_full_unstemmed	Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi
title_sort	modeling analysis of gst (glutathione-s-transferases) from wuchereria bancrofti and brugia malayi
description	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.
publisher	Biomedical Informatics Publishing Group
publishDate	2005
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891627/
_version_	1611397232566730752

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

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