Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein.
Fiche publication
Date publication
mars 2016
Journal
Biochemistry
Auteurs
Membres identifiés du Cancéropôle Est :
Dr KIEFFER Bruno, Dr ROCHEL-GUIBERTEAU Natacha, Dr OSZ-PAPAI Judit
Tous les auteurs :
Belorusova AY, Osz J, Petoukhov MV, Peluso-Iltis C, Kieffer B, Svergun DI, Rochel N
Lien Pubmed
Résumé
Retinoid X receptors (RXRs) are transcription factors with important functions in embryonic development, metabolic processes, differentiation, and apoptosis. A particular feature of RXRs is their ability to act as obligatory heterodimerization partners of class II nuclear receptors. At the same time, these receptors are also able to form homodimers that bind to direct repeat separated by one nucleotide hormone response elements. Since the discovery of RXRs, most of the studies focused on its ligand binding and DNA binding domains, while its N-terminal domain (NTD) harboring a ligand-independent activation function remained poorly characterized. Here, we investigated the solution properties of the NTD of RXRα alone and in the context of the full-length receptor using small-angle X-ray scattering and nuclear magnetic resonance spectroscopy. We report the solution structure of the full-length homodimeric RXRα on DNA and show that the NTD remains highly flexible within this complex.
Mots clés
Animals, Binding Sites, physiology, Cell Line, DNA, chemistry, Insects, Protein Structure, Secondary, Protein Structure, Tertiary, physiology, Retinoid X Receptor alpha, chemistry, X-Ray Diffraction
Référence
Biochemistry. 2016 Mar;55(12):1741-8