Structural insights into the mechanisms of agonism and antagonism in oestrogen receptor isoforms.
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.
Hubbard
R E
RE
Structural Biology Laboratory, Chemistry Department, University of York, YO10 5DD, York, UK. rod@ysbl.york.ac.uk
Pike
A C
AC
Brzozowski
A M
AM
Walton
J
J
Bonn
T
T
Gustafsson
J A
JA
Carlquist
M
M
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
D008024:Ligands; D011960:Receptors, Estrogen; D020845:Selective Estrogen Receptor Modulators; D004958:Estradiol