TY - JOUR
T1 - Molecular docking study of aminoacyl-tRNA synthetases with ligand molecules from four different scaffolds
AU - Bharatham, Nagakumar
AU - Bharatham, Kavitha
AU - Lee, Yuno
AU - Kim, Songmi
AU - Lazar, Prettina
AU - Back, Ayoung
AU - Park, Chanin
AU - Eum, Heesung
AU - Ha, Hyun Joon
AU - Yun, Sae Young
AU - Lee, Won Koo
AU - Kim, Sunghoon
AU - Lee, Keun Woo
PY - 2010/3
Y1 - 2010/3
N2 - Aminoacyl-tRNA synthetases (aaRSs) play vital roles in protein biosynthesis of living organisms and are interesting antibacterial drug targets. In order to find out new inhibitor candidate molecules as antibacterial agent, the binding modes of the candidate molecules were investigated at the active sites of aaRSs by molecular docking study. The docking simulations were performed with 48 compounds from four different scaffolds into the eight different aaRSs. The results show that scaffolds 3 and 4 compounds have consistently better binding capabilities, specifically for HisRS (E. coll) and IleRS (S. aureus). The binding modes of the best compounds with the proteins were well compatible with those of two ligands in crystal structures. Therefore, we expect that the final compounds we present may have reasonable aaRS inhibitory activity.
AB - Aminoacyl-tRNA synthetases (aaRSs) play vital roles in protein biosynthesis of living organisms and are interesting antibacterial drug targets. In order to find out new inhibitor candidate molecules as antibacterial agent, the binding modes of the candidate molecules were investigated at the active sites of aaRSs by molecular docking study. The docking simulations were performed with 48 compounds from four different scaffolds into the eight different aaRSs. The results show that scaffolds 3 and 4 compounds have consistently better binding capabilities, specifically for HisRS (E. coll) and IleRS (S. aureus). The binding modes of the best compounds with the proteins were well compatible with those of two ligands in crystal structures. Therefore, we expect that the final compounds we present may have reasonable aaRS inhibitory activity.
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U2 - 10.5012/bkcs.2010.31.03.606
DO - 10.5012/bkcs.2010.31.03.606
M3 - Article
AN - SCOPUS:77951810651
VL - 31
SP - 606
EP - 610
JO - Bulletin of the Korean Chemical Society
JF - Bulletin of the Korean Chemical Society
SN - 0253-2964
IS - 3
ER -