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Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
Published on: September 21, 2011
Bisphenol-A can bind to human glucocorticoid receptor as an agonist: an in silico study
G K Prasanth1, L M Divya, C Sadasivan
1Department of Biotechnology and Microbiology, Kannur University, Thalassery Campus, Palayad P.O., Kannur, Kerala-670661, India.
Abstract:
Bisphenol-A (BPA) is a primary monomer in polycarbonate plastics and epoxy resins. BPA may be released into the environment following its formation via hydrolysis of ester bonds of the polymers. It has been detected in human plasma, placenta, amniotic fluid, amniotic chord, urine and saliva. BPA disrupts normal cell function by acting as an estrogen agonist as well as an androgen antagonist. The present study was carried out to investigate whether BPA can bind to human glucocorticoid receptor (GR) and elucidate its mode of interaction. BPA has been successfully docked in silico into the ligand binding site of GR using the program Discovery Studio 2.0. The structure has been compared with other agonist and antagonist bound structures of GR. It is found that the mode of interactions and binding energy of BPA were similar to that of DEXA and cortisol, two known agonists of GR. This reveals that BPA can bind to GR as an agonist. Hence, BPA may produce biological effects similar to that produced by glucocorticoids.
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