Publication Abstract from PubMed
A receptor-binding assay and X-ray crystal structure analysis demonstrated that the endocrine disruptor bisphenol A (BPA) strongly binds to human estrogen-related receptor gamma (ERRgamma). BPA is well anchored to the ligand-binding pocket, forming hydrogen bonds with its two phenol-hydroxyl groups. In this study, we found that 4-alpha-cumylphenol lacking one of its phenol-hydroxyl groups also binds to ERRgamma very strongly. The 2.0 A crystal structure of the 4-alpha-cumylphenol/ERRgamma complex clearly revealed that ERRgamma's Leu345-beta-isopropyl plays a role in the tight binding of 4-alpha-cumylphenol and BPA, rotating in a back-and-forth induced-fit manner.
ERRgamma tethers strongly bisphenol A and 4-alpha-cumylphenol in an induced-fit manner.,Matsushima A, Teramoto T, Okada H, Liu X, Tokunaga T, Kakuta Y, Shimohigashi Y Biochem Biophys Res Commun. 2008 Aug 29;373(3):408-13. Epub 2008 Jun 26. PMID:18582436[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
