Tomas Bonn

TL;DR: The crystal structures of the LBD of ER in complex with the endogenous oestrogen, 17β-oestradiol, and the selective antagonist raloxifene provide a molecular basis for the distinctive pharmacophore of the ER and its catholic binding properties.

TL;DR: The three‐dimensional structure of the oestrogen receptor beta isoform (ERβ) ligand‐binding domain (LBD) in the presence of the phyto‐oestrogen genistein and the antagonist raloxifene is reported.

TL;DR: The structures of the liver X receptor LXRβ (NR1H2) have been determined in complexes with two synthetic ligands, T0901317 and GW3965, to 2.1 and 2.4 Å, respectively, revealing a flexible ligand-binding pocket that can adjust to accommodate fundamentally different ligands.

TL;DR: Results suggest indazoles such as 13 may have an improved profile for potential use as a therapeutic agent, and the lack of TG effect of 13 correlated with its inability to increase liver fatty acid synthase (FAS) gene expression.

TL;DR: Three-dimensional structures determined of the ligand-binding domain of the oestrogen receptor in complexes with a range of receptor agonists and antagonists provide a unique insight into the mechanisms that underlie receptor activation, as well as providing a structural basis for the antagonist action of molecules, such as raloxifene.