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Covalent trapping of methyllycaconitine at the α4-α4 interface of the α4β2 nicotinic acetylcholine receptor: antagonist binding site and mode of receptor inhibition revealed

Absalom, Nathan; Quek, Gracia X J; Lewis, Trevor M.; Qudah, Taima; von Arenstorff, Ida; Ambrus, Joseph; Harpsoe, Kaspar; Karim, Nasiara; Balle, Thomas; McLeod, Malcolm; Chebib, Mary


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

CollectionsANU Research Publications
Date published: 2013
Type: Journal article
Source: Journal of Biological Chemistry
DOI: 10.1074/jbc.M113.475053
Access Rights: Open Access


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