Molecular docking and 3D-QSAR on 2-(oxalylamino) benzoic acid and its analogues as protein tyrosine phosphatase 1B inhibitors.
In this paper, molecular docking technique was used to investigate the binding conformation of twelve 2-(oxalylamino) benzoic acid (OBA) inhibitors in the active site of PTP1B. The predicted binding affinities are linearly correlated to the experimental values (r(2)=0.859). Furthermore, comparative molecular field analysis (CoMFA) was conducted based on the binding conformation predicted by molecular docking. The predicted CoMFA model has satisfactory statistical significance and good actual predicted power. The information from molecular docking and CoMFA may give us some valuable hints to the optimization of lead compounds.
Zhou
Mei
M
College of Chemistry and Chemical Engineering, Graduate University of Chinese Academy of Sciences, PO Box 4588, Beijing 100049, PR China.
Ji
Mingjuan
M
D010129:4-Aminobenzoic Acid / Q000138:chemical synthesis / Q000494:pharmacology*; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors*; D021281:Quantitative Structure-Activity Relationship; D062366:para-Aminobenzoates
D004791:Enzyme Inhibitors; D062366:para-Aminobenzoates; C516607:PTPN1 protein, human; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases; D010129:4-Aminobenzoic Acid