Structural aspects of agonism and antagonism in the oestrogen receptor

A. C.W. Pike, A. M. Brzozowski, J. Walton, R. E. Hubbard, T. Bonn, J. A. Gustafsson, M. Carlquist

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

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 underline receptor activation, as well as providing a structural basis for the antagonist action of molecules, such as raloxifene.

Original languageEnglish (US)
Pages (from-to)396-400
Number of pages5
JournalBiochemical Society transactions
Volume28
Issue number4
DOIs
StatePublished - 2000

Keywords

  • Activation function 2
  • Ligand binding
  • Steroid receptor
  • Transcription factor

ASJC Scopus subject areas

  • Biochemistry

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