| Literature DB >> 18582436 |
Ayami Matsushima1, Takamasa Teramoto, Hiroyuki Okada, Xiaohui Liu, Takatoshi Tokunaga, Yoshimitsu Kakuta, Yasuyuki Shimohigashi.
Abstract
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.Entities:
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Year: 2008 PMID： 18582436 DOI： 10.1016/j.bbrc.2008.06.050
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575