期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 28, 期 -, 页码 396-400出版社
PORTLAND PRESS LTD
DOI: 10.1042/0300-5127:0280396
关键词
activation function 2; ligand binding; steroid receptor; transcription factor
We have determined the three-dimensional structures of both alpha- and beta-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 hind 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.
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