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- Birnir, Bryndis, et al.
(author)
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Nature of the 5' residue in the M2 domain affects function of the human alpha 1 beta 1 GABAA receptor.
- 1997
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In: Synapse. - 0887-4476 .- 1098-2396. ; 26:3, s. 324-7
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Journal article (peer-reviewed)abstract
- The effects on the functional properties of the alpha 1 beta 1 GABAA receptor when the 5' (alpha 1 Val260; beta 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 5' amino acids in the M2 region have a role in the conformational changes that occur within the alpha 1 beta 1 GABAA receptor in response to GABA.
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