9
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

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

      Insect Biochemistry and Molecular Biology

      Amino Acid Sequence, Animals, DNA-Binding Proteins, chemistry, metabolism, physiology, Drosophila Proteins, Humans, Insects, Ligands, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, Receptors, Retinoic Acid, Receptors, Steroid, Retinoid X Receptors, Trans-Activators, Transcription Factors, Vertebrates

      Read this article at

      ScienceOpenPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          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.

          Related collections

          Author and article information

          Journal
          10876110

          Comments

          Comment on this article