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

Eur J Cancer. 2000 Sep;36 Suppl 4:S17-8. doi: 10.1016/s0959-8049(00)00207-0.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Estradiol / pharmacology
  • Humans
  • Ligands
  • Receptors, Estrogen / agonists
  • Receptors, Estrogen / antagonists & inhibitors
  • Receptors, Estrogen / chemistry*
  • Selective Estrogen Receptor Modulators / pharmacology

Substances

  • Ligands
  • Receptors, Estrogen
  • Selective Estrogen Receptor Modulators
  • Estradiol