Abstract
Neuronal nicotinic acetylcholine receptors are a prototype of ligand-gated channels that mediate transmission in the central and peripheral nervous system. Structure-function studies performed at the amino acid level are now unraveling the determinant residues either for the properties of the ligand-binding domain or the ionic pore. In this work we review, in the light of the latest finding, the structure-function relationship of these receptors and their implication in neurological diseases.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Allosteric Site
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Animals
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Binding Sites
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Cell Membrane / metabolism
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Central Nervous System / metabolism
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Electrophysiology
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Glycoproteins / metabolism
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Humans
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Ligands
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Models, Biological
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Nervous System Diseases / metabolism
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Neurons / chemistry*
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Neurons / physiology*
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Peripheral Nervous System / metabolism
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Protein Binding
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Protein Conformation
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Protein Structure, Tertiary
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Receptors, Nicotinic / chemistry*
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Receptors, Nicotinic / physiology*
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Structure-Activity Relationship
Substances
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Glycoproteins
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Ligands
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Receptors, Nicotinic