Alternative dimerization interfaces in the glucocorticoid receptor-α ligand binding domain.
Fiche publication
Date publication
avril 2018
Journal
Biochimica et biophysica acta
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DEJAEGERE Annick
Tous les auteurs :
Bianchetti L, Wassmer B, Defosset A, Smertina A, Tiberti ML, Stote RH, Dejaegere A
Lien Pubmed
Résumé
Nuclear hormone receptors (NRs) constitute a large family of multi-domain ligand-activated transcription factors. Dimerization is essential for their regulation, and both DNA binding domain (DBD) and ligand binding domain (LBD) are implicated in dimerization. Intriguingly, the glucocorticoid receptor-α (GRα) presents a DBD dimeric architecture similar to that of the homologous estrogen receptor-α (ERα), but an atypical dimeric architecture for the LBD. The physiological relevance of the proposed GRα LBD dimer is a subject of debate.
Mots clés
Binding free energy, Glucocorticoid receptor, Homodimer, Ligand binding domain, Molecular modeling, Sequence conservation
Référence
Biochim. Biophys. Acta. 2018 Apr 30;: