NMR studies of recombinant active site peptides of the nicotinic acetylcholine receptor
| Autor: | B Ohana, G Navon, J M Gershoni, Yigal Fraenkel |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Atropine
animal structures Magnetic Resonance Spectroscopy Physiology Molecular Sequence Data Receptors Nicotinic law.invention law Drug Discovery Muscarinic acetylcholine receptor medicine Animals Amino Acid Sequence Binding site Peptide sequence Pharmacology Binding Sites General Medicine Recombinant Proteins Nicotinic acetylcholine receptor Nicotinic agonist Biophysics Cholinergic Torpedo Acetylcholine Algorithms medicine.drug |
| Zdroj: | Journal of basic and clinical physiology and pharmacology. 2(3) |
| ISSN: | 0792-6855 |
| Popis: | Interactions of ligands with recombinant cholinergic binding sites have been monitored by NMR. Monitoring the selective T1 relaxation of the protons of acetylcholine, nicotine, d-tubocurarine, and gallamine reveals specific binding to peptide constructs containing the alpha 183-204 or shorter sequences of the nicotinic acetylcholine receptor of Torpedo, Human, Chicken, Xenopus, Mouse, Calf, and Drosophila. The trend of the KD values of the different ligands shows that the binding of the low molecular weight agonists and antagonists is very weak to the Drosophila sequence which is different from the vertebrate sequences in the N and C terminals. Within the vertebrates, the antagonists d-tubocurarine and gallamine display a KD trend different from that of acetylcholine and alpha-bungarotoxin. Specificity of binding is proven by the fact that atropine, a muscarinic inhibitor, binds non-specifically. Temperature dependence indicates a fast exchange limit (T1 bound greater than tau bound) for gallamine bound to the Torpedo alpha 184-200 sequence. This limit should apply also for the other ligands which have weaker binding constants. |
| Databáze: | OpenAIRE |
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