Structure and function of an acetylcholine receptor
| Autor: | Robert M. Stroud, R. A. Lalancette, Robert H. Fairclough, Michael W. Klymkowsky, Joerg Kistler |
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| Rok vydání: | 1982 |
| Předmět: |
Agonist
medicine.drug_class Stereochemistry Neurotoxins Gated Ion Channel Molecular Conformation Biophysics Biology Bungarotoxins Torpedo Models Biological law.invention Turn (biochemistry) law Muscarinic acetylcholine receptor M5 medicine Animals Receptors Cholinergic Binding site Receptor Research Article Acetylcholine receptor |
| Zdroj: | Biophysical Journal. 37:371-383 |
| ISSN: | 0006-3495 |
| DOI: | 10.1016/s0006-3495(82)84685-7 |
| Popis: | Structural analysis of an acetylcholine receptor from Torpedo californica leads to a three-dimensional model in which a "monomeric" receptor is shown to contain subunits arranged around a central ionophoretic channel, which in turn traverses the entire 110 A length of the molecule. The receptor extends approximately 15 A on the cytoplasmic side, 55 A on the synaptic side of the membrane. The alpha-bungarotoxin/agonist binding site is found to be approximately 55 A from the entrance to the central gated ion channel. A hypothesis for the mechanism of AcChR is presented which takes into account the structural and kinetic data, which is testable, and which serves as a focus for future studies on the agonist-induced structure change in AcChR. |
| Databáze: | OpenAIRE |
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