The nuclear receptor ligand-binding domain: structure and function

Curr Opin Cell Biol. 1998 Jun;10(3):384-91. doi: 10.1016/s0955-0674(98)80015-x.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Dimerization
  • Ligands
  • Mice
  • Protein Conformation
  • Receptors, Cytoplasmic and Nuclear / chemistry*
  • Trans-Activators


  • Ligands
  • Receptors, Cytoplasmic and Nuclear
  • Trans-Activators