The nuclear receptor ligand-binding domain: structure and function.
In the past few years our understanding of nuclear receptor action has dramatically improved as a result of the elucidation of the crystal structures of the empty (apo) ligand-binding domains of the nuclear receptor and of complexes formed by the nuclear receptor's ligand-binding domain bound to agonists and antagonists. Furthermore, the concomitant identification and functional analysis of co-regulators (transcriptional intermediary factors [TIFs], comprising co-activators and co-repressors) previously predicted from squelching studies, have deepened this understanding. Recent data have provided the structural basis for the specific recognition of ligands and the molecular mechanisms of agonism and antagonism, enabling us to gain a comprehensive view of the early steps of nuclear receptor action.
Moras
D
D
Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS/INSERM/ULP, Illkirch, France. dino.moras@igbmc.u-strasbg.fr
Gronemeyer
H
H
D000818:Animals; D019281:Dimerization; D008024:Ligands; D051379:Mice; D011487:Protein Conformation; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry*; D015534:Trans-Activators
D008024:Ligands; D018160:Receptors, Cytoplasmic and Nuclear; D015534:Trans-Activators