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Nature of the 5′ residue in the M2 domain affects function of the human α1β1 GABAA receptor

✍ Scribed by B. Birnir; M.L. Tierney; M. Lim; G.B. Cox; P.W. Gage

Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
50 KB
Volume
26
Category
Article
ISSN
0887-4476

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✦ Synopsis

The effects on the functional properties of the a 1 b 1 GABA A receptor when the 58 (a 1 Val260; b 1 Ile255) hydrophobic amino acids in the second transmembrane (M2) region were changed to threonine were examined. In response to a saturating concentration of GABA, the current evoked in mutant receptors showed a decreased rate of desensitization and at equilibrium was a greater fraction of the peak current than in wild-type receptors. The half-saturation concentration of the peak current response to GABA in mutant receptors was comparable to that in wild-type receptors, but the Hill coefficient was reduced to less than one. It was concluded that the 58 amino acids in the M2 region have a role in the conformational changes that occur within the a 1 b 1 GABA A receptor in response to GABA.

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