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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

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Date

2013

Authors

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

Journal Title

Journal ISSN

Volume Title

Publisher

American Society for Biochemistry and Molecular Biology Inc

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

Description

Keywords

Keywords: 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; drug

Citation

URI

http://hdl.handle.net/1885/62348

Collections

ANU Research Publications

Source

Journal of Biological Chemistry

Type

Journal article

Book Title

Entity type

Access Statement

Open Access

License Rights

DOI

10.1074/jbc.M113.475053

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01_Absalom_Covalent_trapping_of_2013.pdf (2.69 MB)

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