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 s tructures of the empty (apo) ligand-binding domains of the nuclear rec eptor and of complexes formed by the nuclear receptor's ligand-binding domain bound to agonists and antagonists. Furthermore, the concomitan t identification and functional analysis of cc-regulators (transcripti onal intermediary factors [TIFs], comprising cc-activators and cc-repr essors) previously predicted from squelching studies, have deepened th is understanding. Recent data have provided the structural basis for t he specific recognition of ligands and the molecular mechanisms of ago nism and antagonism, enabling us to gain a comprehensive view of the e arly steps of nuclear receptor action.