Structural determinants of barium permeation and rectification in non-NMDA glutamate receptor channels.

@article{Dingledine1992StructuralDO,
  title={Structural determinants of barium permeation and rectification in non-NMDA glutamate receptor channels.},
  author={Raymond J Dingledine and Richard I. Hume and Stephen F. Heinemann},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={1992},
  volume={12 10},
  pages={4080-7}
}
A single site in recombinant glutamate receptor channels of the GluR1-GluR4 family has been previously identified as a key regulator of ion permeation. The natural amino acid at this position (arginine in GluR2 but glutamine in GluR1, GluR3, and GluR4) determines both the ability to pass outward current and the divalent cation permeability of kainate-activated receptor channels. By mutagenesis of GluR6, we demonstrated that the same site also controls the ability to pass outward current in… CONTINUE READING

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