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• W2136689007 abstract "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." @default.
• W2136689007 created "2016-06-24" @default.
• W2136689007 creator A5002528693 @default.
• W2136689007 creator A5015654808 @default.
• W2136689007 date "2000-09-01" @default.
• W2136689007 modified "2023-09-25" @default.
• W2136689007 title "Considerations on the structural evidence of a ligand-binding function of ultraspiracle, an insect homolog of vertebrate RXR" @default.
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• W2136689007 doi "https://doi.org/10.1016/s0965-1748(00)00038-2" @default.
• W2136689007 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10876110" @default.
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