Considerations on the structural evidence of a ligand-binding function of ultraspiracle, an insect homolog of vertebrate RXR.

This analysis considers the structural evidence of a ligand-binding function of the nuclear receptor ultraspiracle (USP). The positions and nature of residues in the ligand-binding domain of USP from six higher insects is evaluated in comparison to the function of conserved residues vertebrate receptors that have been co-crystallized with ligand. USP appears to conserve residues that in vertebrate receptors (1) form the hydrophobic ligand-binding pocket, (2) contact oxygen-containing moieties on ligands, such as hydroxyl, keto and carboxyl groups, and (3) in response to ligand-binding conformationally change to form a multi-helix hydrophobic groove for recruitment of transcriptional co-activators. These structural features are consistent with the recent report that USP can bind the epoxymethylfarnesoates (juvenile hormones) and thereupon is induced to change conformation.