Absalom, NathanQuek, Gracia X JLewis, Trevor M.Qudah, Taimavon Arenstorff, IdaAmbrus, JosephHarpsoe, KasparKarim, NasiaraBalle, ThomasMcLeod, MalcolmChebib, Mary2015-12-100021-9258http://hdl.handle.net/1885/62348Background: 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 theAuthor/s retain copyrightKeywords: Nicotinic acetylcholine receptors; Biochemistry; Biology; Amino acids; acetylcholine; methyllycaconitine; nicotinic receptor alpha4beta2; animal cell; article; controlled study; covalent bond; drug binding site; drug protein binding; drug structure; drugCovalent trapping of methyllycaconitine at the α4-α4 interface of the α4β2 nicotinic acetylcholine receptor: antagonist binding site and mode of receptor inhibition revealed201310.1074/jbc.M113.4750532016-02-24