Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.

@article{McCracken2010LinkingOG,
  title={Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.},
  author={Lindsay M. McCracken and Mandy L. McCracken and D H Gong and James R. Trudell and R. Adron Harris},
  journal={ACS chemical neuroscience},
  year={2010},
  volume={1 7},
  pages={482}
}
Glycine receptors (GlyRs) are pentameric ligand-gated ion channels that mediate inhibitory neurotransmission in the brain and spinal cord and are targets of alcohols and anesthetics. The transmembrane (TM) domain of GlyR subunits is composed of four α-helical segments (TM1-4), but there are conflicting data about the orientation of TM3 and TM4 and, therefore, also the proximity of residues (e.g., A288) that are important for alcohol and anesthetic effects. In the present study, we investigated… CONTINUE READING

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