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Eur J Cancer. 2000 Sep;36 Suppl 4:S17-8.

Structural insights into the mechanisms of agonism and antagonism in oestrogen receptor isoforms.

Author information

1
Structural Biology Laboratory, Chemistry Department, University of York, YO10 5DD, York, UK. rod@ysbl.york.ac.uk

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.

PMID:
11056300
DOI:
10.1016/s0959-8049(00)00207-0
[Indexed for MEDLINE]

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