Search: L773:0887 4476 OR L773:1098 2396
> (1995-1999) >
Nature of the 5' re...
Nature of the 5' residue in the M2 domain affects function of the human alpha 1 beta 1 GABAA receptor.
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- Birnir, Bryndis (author)
- John Curtin School of Medical Research, Australian National University
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Tierney, M L (author)
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Lim, M (author)
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Cox, G B (author)
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Gage, P W (author)
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(creator_code:org_t)
- 1997
- 1997
- English.
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In: Synapse. - 0887-4476 .- 1098-2396. ; 26:3, s. 324-7
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Fysiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Physiology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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