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Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings
Data base (NCBI and TIGR) searches are made to retrieve protein sequences of different plant species namely Medicago truncatula, Pisum sativum, Ricinus communis, Arabidopsis thaliana, Vitis vinifera, Glycine max, Daucus carota, Oryza sativa Japonica Group, Arabidopsis lyrata subsp. lyrata, Brachypod...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937584/ https://www.ncbi.nlm.nih.gov/pubmed/24616563 http://dx.doi.org/10.6026/97320630010101 |
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author | Samanta, Aveek Datta, Animesh Kumar Datta, Siraj |
author_facet | Samanta, Aveek Datta, Animesh Kumar Datta, Siraj |
author_sort | Samanta, Aveek |
collection | PubMed |
description | Data base (NCBI and TIGR) searches are made to retrieve protein sequences of different plant species namely Medicago truncatula, Pisum sativum, Ricinus communis, Arabidopsis thaliana, Vitis vinifera, Glycine max, Daucus carota, Oryza sativa Japonica Group, Arabidopsis lyrata subsp. lyrata, Brachypodium distachyon, Oryza sativa Indica Group, Zea mays and careful alignment of derived sequences shows 95% or higher identity. Similarly, DHFR sequence of human being is also retrieved from NCBI. A phylogenetic tree is constructed from different plant and human DHFR domain using the Neighbour – Joining method in MEGA 5.05. Conservation score is performed by using PARALINE. Result suggests that folate binding domain of dihydrofolare reductase is conserved (score 8.06) and excepting some minor variations the basic structure of the domain in both plant species and human being is rather similar. Human DHFR domain contains PEKN sequence near active site, though proline is common for all the selected organisms but the other sequences are different in plants. The plant domain is always associated with TS (Thymidylate synthase). Plant based system is predicted to be an effective model for assessment of MTX (Methotrexate) and other antifolate drugs. |
format | Online Article Text |
id | pubmed-3937584 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-39375842014-03-10 Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings Samanta, Aveek Datta, Animesh Kumar Datta, Siraj Bioinformation Database Data base (NCBI and TIGR) searches are made to retrieve protein sequences of different plant species namely Medicago truncatula, Pisum sativum, Ricinus communis, Arabidopsis thaliana, Vitis vinifera, Glycine max, Daucus carota, Oryza sativa Japonica Group, Arabidopsis lyrata subsp. lyrata, Brachypodium distachyon, Oryza sativa Indica Group, Zea mays and careful alignment of derived sequences shows 95% or higher identity. Similarly, DHFR sequence of human being is also retrieved from NCBI. A phylogenetic tree is constructed from different plant and human DHFR domain using the Neighbour – Joining method in MEGA 5.05. Conservation score is performed by using PARALINE. Result suggests that folate binding domain of dihydrofolare reductase is conserved (score 8.06) and excepting some minor variations the basic structure of the domain in both plant species and human being is rather similar. Human DHFR domain contains PEKN sequence near active site, though proline is common for all the selected organisms but the other sequences are different in plants. The plant domain is always associated with TS (Thymidylate synthase). Plant based system is predicted to be an effective model for assessment of MTX (Methotrexate) and other antifolate drugs. Biomedical Informatics 2014-02-19 /pmc/articles/PMC3937584/ /pubmed/24616563 http://dx.doi.org/10.6026/97320630010101 Text en © 2014 Biomedical Informatics 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 | Database Samanta, Aveek Datta, Animesh Kumar Datta, Siraj Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings |
title | Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings |
title_full | Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings |
title_fullStr | Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings |
title_full_unstemmed | Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings |
title_short | Study on Folate Binding Domain of Dihydrofolate Reductase in Different Plant species and Human beings |
title_sort | study on folate binding domain of dihydrofolate reductase in different plant species and human beings |
topic | Database |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937584/ https://www.ncbi.nlm.nih.gov/pubmed/24616563 http://dx.doi.org/10.6026/97320630010101 |
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