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

• Published in: Biochimica et biophysica acta. General subjects Vol. 1862; no. 8; pp. 1810 - 1825
• Main Authors: Bianchetti, Laurent, Wassmer, Bianca, Defosset, Audrey, Smertina, Anna, Tiberti, Marion L., Stote, Roland H., Dejaegere, Annick
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.08.2018; Elsevier
• Subjects: Animals; Binding free energy; Binding Sites; crystals; dimerization; DNA-binding domains; estrogens; germplasm conservation; Gibbs free energy; Glucocorticoid receptor; Homodimer; hormone receptors; Humans; Life Sciences; Ligand binding domain; Ligands; Mice; Models, Molecular; Molecular modeling; Protein Binding; Protein Conformation; Protein Domains; Protein Multimerization; Quantitative Methods; Receptors, Glucocorticoid - chemistry; Receptors, Glucocorticoid - metabolism; Sequence conservation; therapeutics; transcription factors; Homodimer; Binding free energy; Sequence conservation; Ligand binding domain; Molecular modeling; Glucocorticoid receptor

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 recepto...