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 language | English |
|---|---|
| Pages (from-to) | 408-413 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 373 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Aug 29 2008 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
ERRγ tethers strongly bisphenol A and 4-α-cumylphenol in an induced-fit manner. / Matsushima, Ayami; Teramoto, Takamasa; Okada, Hiroyuki; Liu, Xiaohui; Tokunaga, Takatoshi; Kakuta, Yoshimitsu; Shimohigashi, Yasuyuki.
In: Biochemical and Biophysical Research Communications, Vol. 373, No. 3, 29.08.2008, p. 408-413.Research output: Contribution to journal › Article
}
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.
UR - http://www.scopus.com/inward/record.url?scp=48949115132&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=48949115132&partnerID=8YFLogxK
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 -