A docking modelling rationally predicts strong binding of bisphenol A to estrogen-related receptor gamma.
A computer-aided docking study was carried out to quickly clarify the binding structure of the ligand-receptor complex between bisphenol A (BPA), a well-known endocrine disruptor, and estrogen-related receptor gamma (ERRgamma). The resulting complex indicated that BPA binds to the ligand-binding pocket of ERRgamma without any disruptions of the activation conformation.
Nose
Takeru
T
Laboratory of Structure-Function Biochemistry, Department of Chemistry, Faculty of Sciences, Kyushu University, Fukuoka 812-8581, Japan. nosescc@mbox.nc.kyushu-u.ac.jp
Shimohigashi
Yasuyuki
Y
D001559:Benzhydryl Compounds; D001665:Binding Sites; D004968:Estrogens, Non-Steroidal / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010636:Phenols / Q000737:chemistry*; D011960:Receptors, Estrogen / Q000737:chemistry / Q000378:metabolism*; D000098826:Bisphenol A Compounds
D001559:Benzhydryl Compounds; D004968:Estrogens, Non-Steroidal; D010636:Phenols; D011960:Receptors, Estrogen; C006780:bisphenol A; D000098826:Bisphenol A Compounds