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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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Formato: | Texto |
Lenguaje: | English |
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Biomedical Informatics Publishing Group
2005
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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. |
format | Text |
id | pubmed-1891627 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | Biomedical Informatics Publishing Group |
record_format | MEDLINE/PubMed |
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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