Abstract
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.
Original language | English |
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Pages (from-to) | 26521-26532 |
Number of pages | 12 |
Journal | Journal of Biological Chemistry |
Volume | 288 |
Issue number | 37 |
DOIs | |
Publication status | Published - 13 Sept 2013 |