Identifying the binding site of novel methyllycaconitine (MLA) analogs at α4β2 nicotinic acetylcholine receptors

Quek, Gracia X J; Lin, Diana S-H; Halliday, Jill; Absalom, Nathan; Ambrus, Joseph; Thompson, Andrew J; Lochner, Martin; Lummis, Sarah; McLeod, Malcolm; Chebib, Mary

Identifying the binding site of novel methyllycaconitine (MLA) analogs at α4β2 nicotinic acetylcholine receptors

Date

2010

Authors

Quek, Gracia X J

Lin, Diana S-H

Halliday, Jill

Absalom, Nathan

Ambrus, Joseph

Thompson, Andrew J

Lochner, Martin

Lummis, Sarah

McLeod, Malcolm

Chebib, Mary

Publisher

American Chemical Society

Abstract

Neuronal nicotinic acetylcholine receptors (nAChR) are ligand gated ion channels that mediate fast synaptic transmission. Methyllycaconitine (MLA) is a selective and potent antagonist of the 7 nAChR, and its anthranilate ester side-chain is important for