Allosteric mechanisms in normal and pathological nicotinic acetylcholine receptors.
Recent chemical and advanced structural studies on site-directed and naturally occurring pathological mutants of individual members of the multigene family of nicotinic acetylcholine receptors have yielded structure-function relationships supporting indirect 'allosteric' interactions between the acetylcholine-binding sites and the ion channel in signal transduction.
Changeux
J
J
Laboratoire de Neurobiologie Moléculaire, Institut Pasteur, 25 rue du Dr Roux, 75724 Cedex 15, Paris, France. changeux@pasteur.fr
Edelstein
S J
SJ
D000494:Allosteric Regulation; D000495:Allosteric Site; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000502:physiology; D017173:Caenorhabditis elegans / Q000502:physiology; D003244:Consciousness Disorders / Q000378:metabolism; D005544:Forecasting; D015801:Helminth Proteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D051379:Mice; D018345:Mice, Knockout; D008822:Mice, Transgenic; D023421:Models, Animal; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000502:physiology*; D018722:Nicotinic Agonists / Q000494:pharmacology; D018733:Nicotinic Antagonists / Q000494:pharmacology; D011487:Protein Conformation; D021122:Protein Subunits; D011978:Receptors, Nicotinic / Q000737:chemistry / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D012907:Smoking / Q000378:metabolism; D013329:Structure-Activity Relationship; D014101:Torpedo / Q000502:physiology
D015801:Helminth Proteins; D009419:Nerve Tissue Proteins; D018722:Nicotinic Agonists; D018733:Nicotinic Antagonists; D021122:Protein Subunits; D011978:Receptors, Nicotinic