Characterization of the ligand-binding domain of the ecdysteroid receptor from Drosophila melanogaster.

@article{Grebe2003CharacterizationOT,
  title={Characterization of the ligand-binding domain of the ecdysteroid receptor from Drosophila melanogaster.},
  author={Marco Grebe and Sabina Przibilla and Vincent C. Henrich and Margarethe Spindler-Barth},
  journal={Biological chemistry},
  year={2003},
  volume={384 1},
  pages={105-16}
}
Mutants created by site-directed mutagenesis were used to elucidate the function of amino acids involved in ligand binding to ecdysteroid receptor (EcR) and heterodimer formation with ultraspiracle (USP). The results demonstrate the importance of the C-terminal part of the D-domain and helix 12 of EcR for hormone binding. Some amino acids are involved either in ligand binding to EcR (E476, M504, D572, I617, N626) or ligand-dependent heterodimerization as determined by gel mobility shift assays… CONTINUE READING

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