Structure of the agonist-binding site of the nicotinic acetylcholine receptor. [3H]acetylcholine mustard identifies residues in the cation-binding subsite.
Open Access
- 1 December 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (34) , 23354-23364
- https://doi.org/10.1016/s0021-9258(18)54504-x
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Mapping and modification of an antibody hapten binding site: a site-directed mutagenesis study of McPC603Biochemistry, 1991
- A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTXNeuron, 1990
- Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: [3H]chlorpromazine labels homologous residues in the .beta. and .delta. chainsBiochemistry, 1987
- The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunitsFEBS Letters, 1986
- Structural homology of Torpedo californica acetylcholine receptor subunitsNature, 1983
- Conformations of Torpedo acetylcholine receptor associated with ion transport and desensitizationBiochemistry, 1982
- AGONISTS OF TORPEDO NICOTINIC RECEPTORS: ESSENTIAL ROLE OF A POSITIVE CHARGEAnnals of the New York Academy of Sciences, 1980
- Permeability control by cholinergic receptors in Torpedo postsynaptic membranes: agonist dose-response relations measured at second and millisecond timesBiochemistry, 1980
- Interactions of Acetylcholine Mustard with AcetylcholinesteraseJournal of Pharmaceutical Sciences, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970