Nature of the 5? residue in the M2 domain affects function of the human ?1?1 GABAA receptor

Autor:	Michelle Lim, Bryndis Birnir, Peter W. Gage, M L Tierney, Graeme B. Cox
Rok vydání:	1997
Předmět:	chemistry.chemical_classification Beta-1 adrenergic receptor Cellular and Molecular Neuroscience Biochemistry GABAA receptor Chemistry Biophysics Ligand-gated ion channel Threonine Receptor Amino acid Cys-loop receptors GABAA-rho receptor
Zdroj:	Synapse. 26:324-327
ISSN:	1098-2396 0887-4476
DOI:	10.1002/(sici)1098-2396(199707)26:3<324::aid-syn13>3.0.co;2-v
Popis:	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.
Databáze:	OpenAIRE
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