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 agon ists and antagonists on the structure of ER alpha- and ER beta -LBDs are ex amined. In addition, the findings from structural studies of ER-LBD in comp lex with peptide fragments corresponding to the NR-box II and III modules o f the p160 coactivator TIF2 are discussed in the context of the assembly of ER:coactivator complexes. Together these studies have broadened our unders tanding of ER function by providing a unique insight into ER's ligand speci ficity, it's ability to interact with coactivators and the structural chang es that underlie receptor agonism and antagonism. (C) 2000 Elsevier Science Ltd. All rights reserved.