Research Article: Cell-free Production of the Extracellular Domain of the Nicotinic Acetylcholine Receptor

Date Published: April , 2009

Publisher: A.I. Gordeyev

Author(s): E.N. Lyukmanova, G.S. Kopeina, M.A. Shulepko, Z.O. Shenkarev, A.S. Arseniev, D.A. Dolgikh, M.P. Kirpichnikov.



Partial Text

The nicotinic acetylcholine receptor (nAChR) is a ligand-gated ion channel which is incorporated into the postsynaptic membrane of neurons [1]. NAChR is composed of five homologous subunits, whose transmembrane domains form an ion pore and the N-terminal domains contain the binding sites for the ligand (Fig.1). One of the most common subtypes of nAChR receptor in mammalian nervous systems is a homopentameric, α7 nAChR (α7nAChR), and several neurodegenerative disorders are associated with its dysfunction [2]. An effective system for the production of the individual subunits and other domains of nAChR is a prerequisite for studies focused on the receptor itself, and for the design of biomedical drugs to be used in the treatment of the disease. The tendency of these proteins to form insoluble aggregates in solution makes the development of such systems difficult [3].

This work was financially supported by the Russian Academy of Sciences (The program “Cell and Molecular Biology”), Russian Foundation for Basic Research, and by a grant from the President of the Russian Federation “young scientist” MK-6386.2008.4.