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XB-ART-15294
Neuroreport 1998 Jan 26;92:327-31. doi: 10.1097/00001756-199801260-00027.
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A tetrameric subunit stoichiometry for a glutamate receptor-channel complex.

Mano I , Teichberg VI .


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The structure of glutamate receptor-channel (GluR) subunits has recently been shown to differ from that of other ligand-gated channels and to contain a voltage-gated channel-like pore-forming motif. The view that the structure of GluR complexes is similar to the pentameric structure of other ligand-gated channels was questioned here. Studies of the response properties of the GluR1 subunit of the AMPA subtype of GluRs, co-expressed in Xenopus oocytes with its L646A mutant, which differs only by a greatly reduced sensitivity to quisqualate, provide new evidence suggesting that the GluR1 homomeric receptor channel has a tetrameric structure.

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Species referenced: Xenopus
Genes referenced: gria1