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• W2017347334 abstract "Evidence is presented that the estrogen antagonist 4-hydroxytamoxifen (HT) can occupy not only the core binding pocket within the ligand-binding domain of estrogen receptor (ER) β but also a second site on its surface. The crystal structure of the ligand-binding domain (LBD) associated with HT was determined to 2.2 Å and revealed two molecules of HT bound to the protein. One was located in the consensus ligand-binding pocket, whereas the other bound to a site that overlaps with the hydrophobic groove of the coactivator recognition surface. Relative to the ERα-tamoxifen structure, helix 12 has been displaced from the coactivator recognition surface and occupies a unique position. Although it has been demonstrated that association of the antagonist with the core ligand-binding pocket is sufficient to induce an antagonist ligand-binding domain conformation, this structure suggests that small molecules may directly antagonize receptor–coactivator interactions. These results provide a direct demonstration of two binding sites for HT in ERβ, as has been previously suggested for ERα by using biochemical methods, and represent a crystal structure of a small nonpeptide molecule occupying the coactivator recognition site." @default.
• W2017347334 created "2016-06-24" @default.
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• W2017347334 date "2006-06-27" @default.
• W2017347334 modified "2023-10-10" @default.
• W2017347334 title "A second binding site for hydroxytamoxifen within the coactivator-binding groove of estrogen receptor β" @default.
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• W2017347334 doi "https://doi.org/10.1073/pnas.0510596103" @default.
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