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

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dc.contributor.authorSalgado-Moran, G.
dc.contributor.authorRamirez-Tagle, R.
dc.contributor.authorGlossman-Mitnik, D.
dc.contributor.authorRuiz-Nieto, S.
dc.contributor.authorKishore-Deb, P.
dc.contributor.authorBunste, M.
dc.contributor.authorLobos-Gonzalez, F.
dc.date.accessioned2023-05-15T16:13:26Z
dc.date.available2023-05-15T16:13:26Z
dc.date.issued2013
dc.descriptionIndexación: Scopus.es
dc.description.abstractThe 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.es
dc.description.urihttps://www.hindawi.com/journals/jchem/2013/601270/
dc.identifier.citationJournal of Chemistry, 2013, Article number 601270es
dc.identifier.doi10.1155/2013/601270
dc.identifier.issn2090-9071
dc.identifier.urihttps://repositorio.unab.cl/xmlui/handle/ria/49628
dc.language.isoenes
dc.publisherHindawies
dc.rights.licenseAttribution 3.0 Unported (CC BY 3.0)
dc.rights.urihttps://www.hindawi.com/journals/jchem/2013/601270/#copyright
dc.subjectContainer Closureses
dc.subjectIntegrity Testses
dc.subjectPackaginges
dc.titleDocking studies of binding of ethambutol to the C-terminal domain of the arabinosyltransferase from mycobacterium tuberculosises
dc.typeArtículoes
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