Alternative dimerization interfaces in the glucocorticoid receptor-α ligand binding domain.

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

https://www.ncbi.nlm.nih.gov/pubmed/29723544

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;: