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Structural and Electrostatic Properties of the 5-HT3 Receptor Pore Revealed by Substituted Cysteine Accessibility Mutagenesis*
 

Summary: Structural and Electrostatic Properties of the 5-HT3 Receptor Pore
Revealed by Substituted Cysteine Accessibility Mutagenesis*
Received for publication, June 29, 2001, and in revised form, September 11, 2001
Published, JBC Papers in Press, September 13, 2001, DOI 10.1074/jbc.M106066200
David C. Reeves§, Eric N. Goren¶, Myles H. Akabas¶, and Sarah C. R. Lummis
From the Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1GA,
United Kingdom and the ¶Department of Physiology and Biophysics and Department of Neuroscience,
Albert Einstein College of Medicine, Bronx, New York 10461
5-HT3 receptors are members of the Cys loop family of
ligand-gated ion channels. We used the substituted cys-
teine accessibility method to identify amino acid residues
in the channel forming domain, M2 that face the water-
accessible surface and to locate their position in the ion
conduction pathway. Cysteine was substituted for each
residue, one at a time, in the M2 segment (Asp274
­Asp298
).
5-Hydroxytryptamine EC50 values for functional mutants
did not vary from wild type (1.4 0.2 M) by more than
10-fold, and five mutants were nonfunctional. Covalent

  

Source: Akabas, Myles - Department of Physiology and Biophysics, Albert Einstein College of Medicine, Yeshiva University

 

Collections: Biology and Medicine