A structural biologist's view of the oestrogen receptor.
Here we review the results that have emerged from our structural studies on the oestrogen receptor ligand-binding domain (ER-LBD). The effects of agonists and antagonists on the structure of ERalpha- and ERbeta-LBDs are examined. In addition, the findings from structural studies of ER-LBD in complex with peptide fragments corresponding to the NR-box II and III modules of the p160 coactivator TIF2 are discussed in the context of the assembly of ER:coactivator complexes. Together these studies have broadened our understanding of ER function by providing a unique insight into ER's ligand specificity, it's ability to interact with coactivators and the structural changes that underlie receptor agonism and antagonism.
Pike
A C
AC
Structural Biology Laboratory, Chemistry Department, University of York, York YO10 5DD, Heslington, UK.
Brzozowski
A M
AM
Hubbard
R E
RE
D001665:Binding Sites; D019281:Dimerization; D006801:Humans; D008024:Ligands; D009687:Nuclear Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011960:Receptors, Estrogen / Q000819:agonists / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D020845:Selective Estrogen Receptor Modulators / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism
D008024:Ligands; D009687:Nuclear Proteins; D011960:Receptors, Estrogen; D020845:Selective Estrogen Receptor Modulators; D014157:Transcription Factors