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GABAA Receptor M2M3 Loop Secondary Structure and Changes in Accessibility during Channel Gating*
 

Summary: GABAA Receptor M2M3 Loop Secondary Structure and Changes in
Accessibility during Channel Gating*
Received for publication, June 25, 2002, and in revised form, September 3, 2002
Published, JBC Papers in Press, September 10, 2002, DOI 10.1074/jbc.M206321200
Amal K. Bera, Maya Chatav, and Myles H. Akabas
From the Departments of Physiology & Biophysics and of Neuroscience, Albert Einstein College of Medicine,
Bronx, New York 10461
The -aminobutyric acid type A (GABAA) receptor
M2M3 loop structure and its role in gating were inves-
tigated using the substituted cysteine accessibility
method. Residues from 1Arg-273 to 1Ile-289 were mu-
tated to cysteine, one at a time. MTSET or MTSES
reacted with all mutants from 1R273C to 1Y281C, ex-
cept 1P277C, in the absence and presence of GABA. The
MTSET closed-state reaction rate was >1000 liters/
mol-s at 1N274C, 1S275C, 1K278C, and 1Y281C and
was <300 liters/mol-s at 1R273C, 1L276C, 1V279C,
1A280C, and 1A284C. These two groups of residues lie
on opposite sides of an -helix. The fast reacting group
lies on a continuation of the M2 segment channel-lining

  

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

 

Collections: Biology and Medicine