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Nature of the 5' residue in the M2 domain affects function of the human alpha 1 beta 1 GABAA receptor.
John Curtin School of Medical Research, Australian National University.
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1997 (English)In: Synapse, ISSN 0887-4476, E-ISSN 1098-2396, Vol. 26, no 3, 324-7 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1997. Vol. 26, no 3, 324-7 p.
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URN: urn:nbn:se:uu:diva-182792DOI: 10.1002/(SICI)1098-2396(199707)26:3<324::AID-SYN13>3.0.CO;2-VPubMedID: 9183821OAI: oai:DiVA.org:uu-182792DiVA: diva2:560718
Available from: 2012-10-15 Created: 2012-10-15 Last updated: 2012-10-15

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