ERRγ tethers strongly bisphenol A and 4-α-cumylphenol in an induced-fit manner

Ayami Matsushima, Takamasa Teramoto, Hiroyuki Okada, Xiaohui Liu, Takatoshi Tokunaga, Yoshimitsu Kakuta, Yasuyuki Shimohigashi

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57 Citations (Scopus)

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 γ (ERRγ). 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-α-cumylphenol lacking one of its phenol-hydroxyl groups also binds to ERRγ very strongly. The 2.0 Å crystal structure of the 4-α-cumylphenol/ERRγ complex clearly revealed that ERRγ's Leu345-β-isopropyl plays a role in the tight binding of 4-α-cumylphenol and BPA, rotating in a back-and-forth induced-fit manner.

Original languageEnglish
Pages (from-to)408-413
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume373
Issue number3
DOIs
Publication statusPublished - Aug 29 2008

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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