Comparison of the toxin binding sites of the nicotinic acetylcholine receptor from Drosophila to human
| Autor: | Jonathan M. Gershoni, Bella Ohana |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
medicine.medical_specialty
Recombinant Fusion Proteins Xenopus Receptors Nicotinic Biology Protein Engineering Torpedo Biochemistry law.invention Mice Ganglion type nicotinic receptor Species Specificity law Internal medicine Muscarinic acetylcholine receptor M5 medicine Animals Humans Cobra Neurotoxin Proteins Binding site Acetylcholine receptor Binding Sites Bungarotoxins Nicotinic acetylcholine receptor Endocrinology Nicotinic agonist Cattle Drosophila Alpha-4 beta-2 nicotinic receptor Chickens |
| Zdroj: | Biochemistry. 29:6409-6415 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00479a011 |
| Popis: | Recombinant toxin binding proteins have been previously found to provide a convenient experimental system for the study of receptor-ligand recognition (Aronheim et al., 1988). Here, this system has been used to produce the binding sites of the cholinergic receptor derived from seven organisms, Torpedo californica, Xenopus, chick, mouse, calf, human, and Drosophila. These have been compared with respect to their toxin binding capacity. Scatchard analyses show that the KD values of alpha-bungarotoxin binding to the above sites are 63, 536, 150, 3200, 6200, 6470, and 1700 nM, respectively. These results reiterate the importance of alpha 183-204 as a ligand binding site. In order to increase the repertoire of sites available for study, chimeric structures were constructed. Through the analysis of such chimeras, some themes of the gross anatomy of the binding site can be learned. A positive subsite followed by a hydrophobic patch preceding a nucleophilic domain appears to be required for efficient toxin binding. |
| Databáze: | OpenAIRE |
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