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In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
In humans, purine de novo synthesis pathway consists of multi-functional enzymes. Nucleotide metabolism enzymes are potential drug targets for treating cancer and autoimmune diseases. Glycinamide ribonucleotide transformylase (GART) is one of the most important trifunctional enzymes involved in puri...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562383/ https://www.ncbi.nlm.nih.gov/pubmed/28855807 http://dx.doi.org/10.1016/j.sjbs.2014.11.008 |
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author | Batool, Sidra Nawaz, Muhammad Sulaman Mushtaq, Gohar Parvaiz, Fahed Kamal, Mohammad A. |
author_facet | Batool, Sidra Nawaz, Muhammad Sulaman Mushtaq, Gohar Parvaiz, Fahed Kamal, Mohammad A. |
author_sort | Batool, Sidra |
collection | PubMed |
description | In humans, purine de novo synthesis pathway consists of multi-functional enzymes. Nucleotide metabolism enzymes are potential drug targets for treating cancer and autoimmune diseases. Glycinamide ribonucleotide transformylase (GART) is one of the most important trifunctional enzymes involved in purine synthesis. Previous studies have demonstrated the role of folate inhibitors against tumor activity. In this present study, three components of GART enzyme were targeted as receptor dataset and in silico analysis was carried out with folate ligand dataset. To accomplish the task, Autodock 4.2 was used for determining the docking compatibilities of ligand and receptor dataset. Taken together, it has been suggested that folate ligands could be potentially used as inhibitors of GART. |
format | Online Article Text |
id | pubmed-5562383 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-55623832017-08-30 In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA Batool, Sidra Nawaz, Muhammad Sulaman Mushtaq, Gohar Parvaiz, Fahed Kamal, Mohammad A. Saudi J Biol Sci Original Article In humans, purine de novo synthesis pathway consists of multi-functional enzymes. Nucleotide metabolism enzymes are potential drug targets for treating cancer and autoimmune diseases. Glycinamide ribonucleotide transformylase (GART) is one of the most important trifunctional enzymes involved in purine synthesis. Previous studies have demonstrated the role of folate inhibitors against tumor activity. In this present study, three components of GART enzyme were targeted as receptor dataset and in silico analysis was carried out with folate ligand dataset. To accomplish the task, Autodock 4.2 was used for determining the docking compatibilities of ligand and receptor dataset. Taken together, it has been suggested that folate ligands could be potentially used as inhibitors of GART. Elsevier 2017-09 2014-11-22 /pmc/articles/PMC5562383/ /pubmed/28855807 http://dx.doi.org/10.1016/j.sjbs.2014.11.008 Text en © 2014 The Authors http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/). |
spellingShingle | Original Article Batool, Sidra Nawaz, Muhammad Sulaman Mushtaq, Gohar Parvaiz, Fahed Kamal, Mohammad A. In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA |
title | In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA |
title_full | In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA |
title_fullStr | In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA |
title_full_unstemmed | In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA |
title_short | In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA |
title_sort | in silico analysis of glycinamide ribonucleotide transformylase inhibition by py873, py899 and dia |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562383/ https://www.ncbi.nlm.nih.gov/pubmed/28855807 http://dx.doi.org/10.1016/j.sjbs.2014.11.008 |
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