title: Structural insights into the mechanisms of agonism and antagonism in oestrogen receptor isoforms.
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.
authors.affiliation: Structural Biology Laboratory, Chemistry Department, University of York, YO10 5DD, York, UK. rod@ysbl.york.ac.uk
authors.forename: R E
authors.initials: RE
authors.lastname: Hubbard
authors.forename: A C
authors.initials: AC
authors.lastname: Pike
authors.forename: A M
authors.initials: AM
authors.lastname: Brzozowski
authors.forename: J
authors.initials: J
authors.lastname: Walton
authors.forename: T
authors.initials: T
authors.lastname: Bonn
authors.forename: J A
authors.initials: JA
authors.lastname: Gustafsson
authors.forename: M
authors.initials: M
authors.lastname: Carlquist
mesh_terms: D004958:Estradiol / Q000494:pharmacology; D006801:Humans; D008024:Ligands; D011960:Receptors, Estrogen / Q000819:agonists / Q000037:antagonists & inhibitors / Q000737:chemistry*; D020845:Selective Estrogen Receptor Modulators / Q000494:pharmacology
chemical_list: D008024:Ligands; D011960:Receptors, Estrogen; D020845:Selective Estrogen Receptor Modulators; D004958:Estradiol