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Structural and functional characterization of the gamma 1 subunit of GABAA/benzodiazepine receptors

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Draguhn,  Andreas
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Werner,  Pia
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Sprengel,  Rolf
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society;
Olfaction Web, Max Planck Institute for Medical Research, Max Planck Society;

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Seeburg,  Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Ymer, S., Draguhn, A., Wisden, W., Werner, P., Keinänen, K., Schofield, P. R., et al. (1990). Structural and functional characterization of the gamma 1 subunit of GABAA/benzodiazepine receptors. The EMBO Journal, 9(10), 3261-3267. doi:10.1002/j.1460-2075.1990.tb07525.x.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-AD59-2
Abstract
The GABAA receptor gamma 1 subunit of human, rat and bovine origin was molecularly cloned and compared with the gamma 2 subunit in structure and function. Both gamma subunit variants share 74% sequence similarity and are prominently synthesized in often distinct areas of the central nervous system as documented by in situ hybridization. When co-expressed with alpha and beta subunits in Xenopus oocytes and mammalian cells, the gamma variants mediate the potentiation of GABA evoked currents by benzodiazepines and help generate high-affinity binding sites for these drugs. However, these sites show disparate pharmacological properties which, for receptors assembled from alpha 1, beta 1 and gamma 1 subunits, are characterized by the conspicuous loss in affinity for neutral antagonists (e.g. flumazenil) and negative modulators (e.g. DMCM). These findings reveal a pronounced effect of gamma subunit variants on GABAA/benzodiazepine receptor pharmacology.