Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

Nature. 1995 Jun 1;375(6530):377-82. doi: 10.1038/375377a0.


The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Biopolymers
  • Computer Graphics
  • Crystallography, X-Ray
  • DNA / metabolism
  • Escherichia coli
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Receptors, Retinoic Acid / chemistry*
  • Receptors, Retinoic Acid / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Retinoid X Receptors
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism
  • Transcriptional Activation


  • Biopolymers
  • Ligands
  • Nuclear Proteins
  • Receptors, Retinoic Acid
  • Recombinant Proteins
  • Retinoid X Receptors
  • Transcription Factors
  • DNA