Modeling the interactions of herbal drugs to beta-ketoacyl ACP synthase of Mycobacterium tuberculosis H37Rv.
J Biomol Struct Dyn
; 25(5): 481-93, 2008 Apr.
Article
em En
| MEDLINE
| ID: mdl-18282003
ABSTRACT
The present paper reports a bio-computational study carried out with the aim of understanding the binding mode of anti-TB herbal ligands onto the homology modeled structure of fatty acid synthase of Mycobacterium tuberculosis (M.tb) H37Rv. Sequence alignment of beta-ketoacyl ACP synthase (KAS) domain of the protein with other related KAS sequences of PDB database revealed high degree of sequence variation. However, the catalytic triad comprising of CHH (cys150-his279-his320) was found to be conserved in the KAS sequence of M.tb H37Rv. The tertiary structure of this protein predicted using genetic algorithm operator in the MODELLER package appeared to give a satisfactory structure for the purpose of studying ligand and substrate binding pockets on the protein. PDB templates complexed with ligands (citric acid and lauric acid) were used for model building. Docking studies carried out with different herbal ligands suggest that, aloe-emodin and nimbin are the best herbal candidates to replace the synthetic drugs 'thiolactomycin/cerulenin'.
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Base de dados:
MEDLINE
Assunto principal:
3-Oxoacil-(Proteína de Transporte de Acila) Sintase
/
Proteínas de Bactérias
/
Modelos Moleculares
/
Estrutura Terciária de Proteína
/
Preparações de Plantas
/
Mycobacterium tuberculosis
/
Antituberculosos
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
J Biomol Struct Dyn
Ano de publicação:
2008
Tipo de documento:
Article