Allosteric Sites and Conformational Transitions of the Acetylcholine Receptor: Models for Short-term Regulation of Receptor Response

  • J. P. Changeux
  • J. Giraudat
  • M. Dennis
  • M. Goeldner
  • C. Hirth
  • C. Mulle
  • F. Révah
  • A. Devillers-Thiéry
  • T. Heidmann
Part of the Wenner-Gren Center International Symposium Series book series (WGCISS)


The word “receptor” is commonly used with two separate significations: for the site complementary to the structure of the chemical messenger and for the protein which carries the site. From a functional point of view, receptor-receptor interactions (Fuxe et al., 1981, 1983, 1986, Agnati et al., 1983a,b, 1984) may be considered as representing interactions between distinct sites for specific ligands without any preconception about the protein components involved. One may thus legitimately distinguish at the cell, or synaptic, level : 1) intramolecular allosteric interactions between topologically distinct sites mediated by a unique protein assembly via conformational transitions (see Monod et al., 1963, 1965, Changeux 1981, Changeux et al., 1976, 1983, 1984) and 2) indirect intermolecular coupling between distinct protein entities transmitted by close contact within the membrane, by electric fields and/or intracellular second messengers. However, even in these last instances at least one allosteric protein integrates the interaction between one primary messenger and the coupling signals produced by another. receptor (see Changeux 1986).


Acetylcholine Receptor Nicotinic Acetylcholine Receptor Cholinergic Receptor Allosteric Transition Electric Organ 
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Copyright information

© The Wenner-Gren Center 1987

Authors and Affiliations

  • J. P. Changeux
  • J. Giraudat
  • M. Dennis
  • M. Goeldner
  • C. Hirth
  • C. Mulle
  • F. Révah
  • A. Devillers-Thiéry
  • T. Heidmann

There are no affiliations available

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