TY - JOUR
T1 - ERRγ tethers strongly bisphenol A and 4-α-cumylphenol in an induced-fit manner
AU - Matsushima, Ayami
AU - Teramoto, Takamasa
AU - Okada, Hiroyuki
AU - Liu, Xiaohui
AU - Tokunaga, Takatoshi
AU - Kakuta, Yoshimitsu
AU - Shimohigashi, Yasuyuki
PY - 2008/8/29
Y1 - 2008/8/29
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bbrc.2008.06.050
DO - 10.1016/j.bbrc.2008.06.050
M3 - Article
C2 - 18582436
AN - SCOPUS:48949115132
VL - 373
SP - 408
EP - 413
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -