Mutational analysis of the structure and function of opioid receptors

Biopolymers. 1999;51(6):440-55. doi: 10.1002/(SICI)1097-0282(1999)51:6<440::AID-BIP6>3.0.CO;2-T.


The cloning of the opioid receptors allows the investigation of receptor domains involved in the peptidic and nonpeptidic ligand interaction and activation of the opioid receptors. Receptor chimera studies and mutational analysis of the primary sequences of the opioid receptors have provided insights into the structural domains required for the ligand recognition and receptor activation. In the current review, we examine the current reports on the possible involvement of extracellular domains and transmembrane domains in the high-affinity binding of peptidic and nonpeptidic ligands to the opioid receptor. The structural requirement for the receptors' selectivity toward different ligands is discussed. The receptor domains involved in the activation and subsequent cellular regulation of the receptors' activities as determined by mutational analysis will also be discussed. Finally, the validity of the conclusions based on single amino acid mutations is examined.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • DNA Mutational Analysis
  • GTP-Binding Proteins / metabolism
  • Ligands
  • Membrane Proteins / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Receptors, Opioid / chemistry
  • Receptors, Opioid / genetics*
  • Receptors, Opioid / metabolism
  • Structure-Activity Relationship


  • Ligands
  • Membrane Proteins
  • Receptors, Opioid
  • GTP-Binding Proteins