Allosteric modulation of muscarinic acetylcholine receptors

Trends Pharmacol Sci. 1995 Jun;16(6):205-12. doi: 10.1016/s0165-6147(00)89023-9.

Abstract

Five subtypes of muscarinic acetylcholine receptors have been identified in mammalian tissues, but the selectivity of ligands that are active at these receptors is low. It is possible, however, that selective compounds may be developed by targeting their allosteric site(s). Important new insights into the mechanism of allosteric control of muscarinic receptors have been obtained recently in investigations of the allosteric effects of neuromuscular blockers, and competition between ligands for the allosteric binding site has now been demonstrated. It is now apparent that the binding site for most allosteric ligands is close to the binding site for acetylcholine but that it is located at a more extracellular position. Stanislav Tucek and Jan Proska discuss the pharmacological implications of ligand interaction at these two sites and the therapeutic possibilities.

Publication types

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

MeSH terms

  • Allosteric Regulation
  • Animals
  • Humans
  • Ligands
  • Receptors, Muscarinic / chemistry
  • Receptors, Muscarinic / drug effects*

Substances

  • Ligands
  • Receptors, Muscarinic