Docking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosis

Guillermo Salgado-Moran, Rodrigo Ramirez-Tagle, Daniel Glossman-Mitnik, Samuel Ruiz-Nieto, Pran Kishore-Deb, Marta Bunster, Francisco Lobos-Gonzalez

Resultado de la investigación: Article

2 Citas (Scopus)

Resumen

The binding of ethambutol to the C-terminal domain of the arabinosyltransferase from Mycobacterium tuberculosis was studied. The analysis was performed using an in silico approach in order to find out, by docking calculations and energy descriptors, the conformer of Ethambutol that forms the most stable complex with the C-terminal domain of arabinosyltransferase. The complex shows that location of the Ethambutol coincides with the cocrystallization ligand position and that amino acid residues ASH1051, ASN740, ASP1052, and ARG1055 should be critical in the binding of Ethambutol to C-terminal domain EmbC.

Idioma originalEnglish
Número de artículo601270
PublicaciónJournal of Chemistry
DOI
EstadoPublished - 2013

Huella dactilar

Ethambutol
Ligands
Amino Acids
arabinosyltransferase

ASJC Scopus subject areas

  • Chemistry(all)

Citar esto

Salgado-Moran, G., Ramirez-Tagle, R., Glossman-Mitnik, D., Ruiz-Nieto, S., Kishore-Deb, P., Bunster, M., & Lobos-Gonzalez, F. (2013). Docking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosis. Journal of Chemistry, [601270]. https://doi.org/10.1155/2013/601270
Salgado-Moran, Guillermo ; Ramirez-Tagle, Rodrigo ; Glossman-Mitnik, Daniel ; Ruiz-Nieto, Samuel ; Kishore-Deb, Pran ; Bunster, Marta ; Lobos-Gonzalez, Francisco. / Docking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosis. En: Journal of Chemistry. 2013.
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abstract = "The binding of ethambutol to the C-terminal domain of the arabinosyltransferase from Mycobacterium tuberculosis was studied. The analysis was performed using an in silico approach in order to find out, by docking calculations and energy descriptors, the conformer of Ethambutol that forms the most stable complex with the C-terminal domain of arabinosyltransferase. The complex shows that location of the Ethambutol coincides with the cocrystallization ligand position and that amino acid residues ASH1051, ASN740, ASP1052, and ARG1055 should be critical in the binding of Ethambutol to C-terminal domain EmbC.",
author = "Guillermo Salgado-Moran and Rodrigo Ramirez-Tagle and Daniel Glossman-Mitnik and Samuel Ruiz-Nieto and Pran Kishore-Deb and Marta Bunster and Francisco Lobos-Gonzalez",
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Salgado-Moran, G, Ramirez-Tagle, R, Glossman-Mitnik, D, Ruiz-Nieto, S, Kishore-Deb, P, Bunster, M & Lobos-Gonzalez, F 2013, 'Docking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosis', Journal of Chemistry. https://doi.org/10.1155/2013/601270

Docking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosis. / Salgado-Moran, Guillermo; Ramirez-Tagle, Rodrigo; Glossman-Mitnik, Daniel; Ruiz-Nieto, Samuel; Kishore-Deb, Pran; Bunster, Marta; Lobos-Gonzalez, Francisco.

En: Journal of Chemistry, 2013.

Resultado de la investigación: Article

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T1 - Docking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosis

AU - Salgado-Moran, Guillermo

AU - Ramirez-Tagle, Rodrigo

AU - Glossman-Mitnik, Daniel

AU - Ruiz-Nieto, Samuel

AU - Kishore-Deb, Pran

AU - Bunster, Marta

AU - Lobos-Gonzalez, Francisco

PY - 2013

Y1 - 2013

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