Human microsomal prostaglandin E synthase-1 (mPGES-1) binding with inhibitors and the quantitative structure-activity correlation.
The detailed structures of microsomal prostaglandin E synthase-1 (mPGES-1) binding with inhibitors have been studied, for the first time, by using a newly developed computational three-dimensional (3D) structural model of mPGES-1 along with a 3D-quantitative structure--activity relationship (3D-QSAR) analysis. The obtained satisfactory binding structures and 3D-QSAR models strongly suggest that the 3D structural model of mPGES-1 is reasonable for study of mPGES-1 binding with inhibitors and for future design of novel mPGES-1 inhibitors.
Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 725 Rose Street, Lexington, Kentucky 40536, USA.
Mohamed Diwan M
MD
AbdulHameed
Adel
A
Hamza
Junjun
J
Liu
Xiaoqin
X
Huang
Chang-Guo
CG
Zhan
D001665:Binding Sites; D015195:Drug Design; D006801:Humans; D019746:Intramolecular Oxidoreductases / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D000071876:Prostaglandin-E Synthases; D021281:Quantitative Structure-Activity Relationship; D055672:Static Electricity
D019746:Intramolecular Oxidoreductases; C000605862:PTGES protein, human; D000071876:Prostaglandin-E Synthases