Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.

@article{Kuhse1993AssemblyOT,
  title={Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.},
  author={Jochen Kuhse and Bodo Laube and D Magalei and Heinrich Betz},
  journal={Neuron},
  year={1993},
  volume={11 6},
  pages={1049-56}
}
The inhibitory glycine receptor (GlyR) is a pentameric protein composed of two types (alpha and beta) of membrane-spanning subunits. Coexpression in Xenopus oocytes of a low affinity mutant of the alpha 2 subunit with the alpha 1 and beta subunits indicated that GlyRs assembled from alpha 1 and alpha 2 polypeptides contain variable subunit ratios, whereas alpha/beta hetero-oligomers have an invariant (3:2) stoichiometry. Analysis of different alpha/beta chimeric constructs revealed that this… CONTINUE READING

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