Please use this identifier to cite or link to this item: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8968
Full metadata record
DC FieldValueLanguage
dc.contributor.authorRamana, Jayashree-
dc.date.accessioned2023-01-05T06:43:45Z-
dc.date.available2023-01-05T06:43:45Z-
dc.date.issued2013-
dc.identifier.urihttp://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8968-
dc.description.abstractAn alarming emergence of multidrug-resistant strains of the tuberculosis pathogen Mycobacterium tuberculosis and continuing high worldwide incidence of tuberculosis has invigorated the search for novel drug targets. The enzyme glutamate racemase (MurI) in bacteria catalyzes the stereoconversion of L-glutamate to D-glutamate which is a component of the peptidoglycan cell wall of the bacterium. The inhibitors targeted against MurI from several bacterial species have been patented and are advocated as promising antibacterial agents. However there are none available against MurI from Mycobacterium tuberculosis, due to the lack of its threedimensional structure. This work accomplished two major objectives. First, the tertiary structure of MtMurI was deduced computationally through homology modeling using the templates from bacterial homologues. It is speculated that like in other Gram-positive bacteria, MtMurI exists as a dimer and many of the protein interactions at the dimer interface are also conserved. Second, potent candidate inhibitors against MtMurI were identified through docking against already known inhibitors in other organismsen_US
dc.language.isoenen_US
dc.publisherJaypee University of Information Technology, Solan, H.P.en_US
dc.subjectGlutamate racemaseen_US
dc.subjectHomology modelingen_US
dc.subjectDockingen_US
dc.subjectDrug resistanceen_US
dc.titleNovel Structural Insights of Glutamate Racemase from Mycobacterium tuberculosis through Modeling and Docking Studiesen_US
dc.typeArticleen_US
Appears in Collections:Journal Articles



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.