Key points are not available for this paper at this time.
Background: Methyllycaconitine is an antagonist at subtypes of the nicotinic acetylcholine receptor. Results: A reactive methyllycaconitine probe was covalently trapped by a cysteine introduced on the complementary face of the α4 subunit and only in the (α4) 3 (β2) 2 nAChR stoichiometry. Conclusion: The α4-α4 interface on the α4β2 nAChR contains a methyllycaconitine binding site. Significance: Defining the molecular interactions of nAChR ligands at the α4-α interface may lead to superior therapeutics. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
Absalom et al. (2013) studied this question.