Antibodies as tools to study the structure of membrane proteins: the case of the nicotinic acetylcholine receptor
Autor: | Conti-Fine Bm, Lei S, Mclane Ke |
---|---|
Rok vydání: | 1996 |
Předmět: |
Models
Molecular Protein Folding Protein Conformation Biophysics Receptors Nicotinic Torpedo Antibodies Antigen-Antibody Reactions Epitopes Ganglion type nicotinic receptor Receptors Glycine Structural Biology Antibody Specificity Muscarinic acetylcholine receptor M5 Animals Glycine receptor Acetylcholine receptor Chemistry Membrane Proteins Bungarotoxins Rats Nicotinic acetylcholine receptor Nicotinic agonist Biochemistry Receptors Glutamate Multigene Family Alpha-4 beta-2 nicotinic receptor Cys-loop receptors |
Zdroj: | Annual review of biophysics and biomolecular structure. 25 |
ISSN: | 1056-8700 |
Popis: | The nicotinic acetylcholine receptor is the prototype of the ionotropic receptor superfamily of proteins, which includes the closely related gamma- aminobutyric acid type A and glycine receptors, and more distantly related serotonin type-3 and glutamate receptors. Several models of the transmembrane topology of the nicotinic acetylcholine receptor subunits were originally proposed based on hydropathy analysis of their deduced amino acid sequences. Antibodies specific to different epitopes of the nicotinic acetylcholine receptor have proven to be valuable probes for examining the validity of those models. Despite important caveats, a viable model for the transmembrane structure and functional topology of the nicotinic acetylcholine receptor subunits has been obtained from the antibody mapping studies. This model, and the associated methodological shortcomings and obstacles that were overcome in the process of its formulation, can legitimately be extended to other members of the ionotropic receptor superfamily and to other membrane proteins as well. |
Databáze: | OpenAIRE |
Externí odkaz: |