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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 human GST in sequence and...

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Autores principales: Bhargavi, Rayavarapu, Vishwakarma, Siddharth, Murty, Upadhyayula Suryanarayana
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891627/
https://www.ncbi.nlm.nih.gov/pubmed/17597848
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author Bhargavi, Rayavarapu
Vishwakarma, Siddharth
Murty, Upadhyayula Suryanarayana
author_facet Bhargavi, Rayavarapu
Vishwakarma, Siddharth
Murty, Upadhyayula Suryanarayana
author_sort Bhargavi, Rayavarapu
collection PubMed
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.
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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 Bioinformation 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.
spellingShingle Hypothesis
Bhargavi, Rayavarapu
Vishwakarma, Siddharth
Murty, Upadhyayula Suryanarayana
Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi
title 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_short 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
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891627/
https://www.ncbi.nlm.nih.gov/pubmed/17597848
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