Structural insights into the mechanisms of agonism and antagonism in oestrogen receptor isoforms

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

Research output: Contribution to journalShort survey

16 Scopus citations

Abstract

Here we summarise the results that have emerged from our structural studies on the oestrogen receptor (ER) ligand-binding domain. We have investigated the conformational effects of a variety of ligands on the structures of both ER isoforms. Each class of ligand (agonists, partial agonists and selective oestrogen receptor modulators) induces a unique conformation in the receptor's ligand-dependent transcriptional activation function. Together these studies have broadened our understanding of ER function by providing a unique insight into ER's ligand specificity and the structural changes that underlie receptor agonism and antagonism. (C) 2000 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)17-18
Number of pages2
JournalEuropean Journal of Cancer
Volume36
Issue numberSUPPL. 4
DOIs
StatePublished - 2000

Keywords

  • Agonist
  • Antagonist
  • Crystal structure
  • ERα
  • ERβ
  • Transactivation

ASJC Scopus subject areas

  • Cancer Research
  • Hematology
  • Oncology

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