We have determined the three-dimensional structures of both α- and β-forms of the ligand-binding domain of the oestrogen receptor (ER) in complexes with a range of receptor agonists and antagonists. Here, we summarize how these structures provide both an understanding of the ER's distinctive pharmacophore and a rationale for its ability to bind a diverse range of chemically distinct compounds. In addition, these studies provide a unique insight into the mechanisms that underlie receptor activation, as well as providing a structural basis for the antagonist action of molecules, such as raloxifene.
Structural aspects of agonism and antagonism in the oestrogen receptor
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A. C. W. Pike, A. M. Brzozowski, J. Walton, R. E. Hubbard, T. Bonn, J-Å. Gustafsson, M. Carlquist; Structural aspects of agonism and antagonism in the oestrogen receptor. Biochem Soc Trans 1 August 2000; 28 (4): 396–400. doi: https://doi.org/10.1042/bst0280396
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