In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013 |
Resumo: | Leishmaniasis is one of the most common form of neglected parasitic disease that affects about 350 million people worldwide. Leishmanias have a trypanothione mediated hydroperoxide metabolism to eliminate endogenous or exogenous oxidative agents. Both of 2-Cys peroxiredoxin (Prx) and glutathione peroxidase type tryparedoxin peroxidase (Px) are the terminal enzymes in the trypanothione dependent detoxification system. Therefore absence of trypanothione redox system in mammals and the sensitivity of trypanosomatids against oxidative stress, enzymes of this pathway are drug targets candidates. In this study, 3D structure of tryparedoxin peroxidase (2-Cys peroxiredoxin type) from Leishmania donovani (LdTXNPx) was described by homology modeling method based on the template of tryparedoxin peroxidase from Crithidia fasciculata and selected compounds were docked to the active site pocket. The quality of the 3D structure of the model was confirmed by various web based validation programs. When compared secondary and tertiary structure of the model, it showed a typical thioredoxin fold containing a central beta-sheet and three alpha-helices. Docking study showed that the selected compound 2 (CID 16073813) interacted with the active site amino acids and binding energy was -118.675 kcal/mol. |
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In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidaseHomology modelingdockingLeishmania donovanitryparedoxin peroxidasehydroperoxide metabolismLeishmaniasis is one of the most common form of neglected parasitic disease that affects about 350 million people worldwide. Leishmanias have a trypanothione mediated hydroperoxide metabolism to eliminate endogenous or exogenous oxidative agents. Both of 2-Cys peroxiredoxin (Prx) and glutathione peroxidase type tryparedoxin peroxidase (Px) are the terminal enzymes in the trypanothione dependent detoxification system. Therefore absence of trypanothione redox system in mammals and the sensitivity of trypanosomatids against oxidative stress, enzymes of this pathway are drug targets candidates. In this study, 3D structure of tryparedoxin peroxidase (2-Cys peroxiredoxin type) from Leishmania donovani (LdTXNPx) was described by homology modeling method based on the template of tryparedoxin peroxidase from Crithidia fasciculata and selected compounds were docked to the active site pocket. The quality of the 3D structure of the model was confirmed by various web based validation programs. When compared secondary and tertiary structure of the model, it showed a typical thioredoxin fold containing a central beta-sheet and three alpha-helices. Docking study showed that the selected compound 2 (CID 16073813) interacted with the active site amino acids and binding energy was -118.675 kcal/mol.Instituto de Tecnologia do Paraná - Tecpar2014-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013Brazilian Archives of Biology and Technology v.57 n.2 2014reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132014000200013info:eu-repo/semantics/openAccessMutlu,Ozaleng2014-04-04T00:00:00Zoai:scielo:S1516-89132014000200013Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2014-04-04T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase |
title |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase |
spellingShingle |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase Mutlu,Ozal Homology modeling docking Leishmania donovani tryparedoxin peroxidase hydroperoxide metabolism |
title_short |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase |
title_full |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase |
title_fullStr |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase |
title_full_unstemmed |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase |
title_sort |
In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase |
author |
Mutlu,Ozal |
author_facet |
Mutlu,Ozal |
author_role |
author |
dc.contributor.author.fl_str_mv |
Mutlu,Ozal |
dc.subject.por.fl_str_mv |
Homology modeling docking Leishmania donovani tryparedoxin peroxidase hydroperoxide metabolism |
topic |
Homology modeling docking Leishmania donovani tryparedoxin peroxidase hydroperoxide metabolism |
description |
Leishmaniasis is one of the most common form of neglected parasitic disease that affects about 350 million people worldwide. Leishmanias have a trypanothione mediated hydroperoxide metabolism to eliminate endogenous or exogenous oxidative agents. Both of 2-Cys peroxiredoxin (Prx) and glutathione peroxidase type tryparedoxin peroxidase (Px) are the terminal enzymes in the trypanothione dependent detoxification system. Therefore absence of trypanothione redox system in mammals and the sensitivity of trypanosomatids against oxidative stress, enzymes of this pathway are drug targets candidates. In this study, 3D structure of tryparedoxin peroxidase (2-Cys peroxiredoxin type) from Leishmania donovani (LdTXNPx) was described by homology modeling method based on the template of tryparedoxin peroxidase from Crithidia fasciculata and selected compounds were docked to the active site pocket. The quality of the 3D structure of the model was confirmed by various web based validation programs. When compared secondary and tertiary structure of the model, it showed a typical thioredoxin fold containing a central beta-sheet and three alpha-helices. Docking study showed that the selected compound 2 (CID 16073813) interacted with the active site amino acids and binding energy was -118.675 kcal/mol. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-04-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89132014000200013 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.57 n.2 2014 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318276097867776 |