Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists.-Reference-Cited by-同舟云学术

Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists.

Published:1994-03 Issue:12 Volume:269 Page:8808-8816
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Sine S.M.,Quiram P.,Papanikolaou F.,Kreienkamp H.J.,Taylor P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. Identification of a novel amino acid alpha-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-binding sites.

2. Structure of the agonist-binding site of the nicotinic acetylcholine receptor. [3H]acetylcholine mustard identifies residues in the cation-binding subsite.

3. An Analog of Lophotoxin Reacts Covalently with Tyr190 in the α-Subunit of the Nicotinic Acetylcholine Receptor

4. Amino acids of the Torpedo marmorata acetylcholine receptor .alpha. subunit labeled by a photoaffinity ligand for the acetylcholine binding site

5. Mapping of the acetylcholine binding site of the nicotinic acetylcholine receptor: [3H]nicotine as an agonist photoaffinity label

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