Lessons learnt from structural studies of the oestrogen receptor.
Over the last 10 years, structural studies of the ligand-binding domains of nuclear hormone receptors have provided a wealth of information on the nature of ligand-binding and its role in receptor activation. This review examines the insights that studies on oestrogen receptor subtypes ERalpha and ERbeta have provided in terms of (1) basis of receptor activation; (2) recruitment of coregulators; (3) hormone recognition; and (4) subtype-selective ligands. It also highlights the implications for the binding of endocrine disruptors.
Pike
Ashley C W
AC
Structural Biology Laboratory, Chemistry Department, University of York, York YO10 5YW, UK. pike@ysbl.york.ac.uk
D000818:Animals; D003461:Crystallography; D004965:Estrogen Antagonists / Q000737:chemistry / Q000494:pharmacology; D047628:Estrogen Receptor alpha / Q000819:agonists / Q000737:chemistry*; D047629:Estrogen Receptor beta / Q000819:agonists / Q000737:chemistry*; D006801:Humans; D008024:Ligands; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D020845:Selective Estrogen Receptor Modulators / Q000494:pharmacology; D015533:Transcriptional Activation / Q000502:physiology
D004965:Estrogen Antagonists; D047628:Estrogen Receptor alpha; D047629:Estrogen Receptor beta; D008024:Ligands; D020845:Selective Estrogen Receptor Modulators