Radial Symmetry in a Chimaeric Glutamate Receptor Pore

@inproceedings{Wilding2014RadialSI,
  title={Radial Symmetry in a Chimaeric Glutamate Receptor Pore},
  author={Timothy J. Wilding and M. Nieblas L{\'o}pez and James E Huettner},
  booktitle={Nature communications},
  year={2014}
}
Ionotropic glutamate receptors comprise two conformationally different A/C and B/D subunit pairs. Closed channels exhibit fourfold radial symmetry in the transmembrane domain (TMD) but transition to twofold dimer-of-dimers symmetry for extracellular ligand binding and N-terminal domains. Here, to evaluate symmetry in open pores we analysed interaction between the Q/R editing site near the pore loop apex and the transmembrane M3 helix of kainate receptor subunit GluK2. Chimeric subunits that… CONTINUE READING

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The authors declare no competing financial interests

N. Eswar, D. Eramian, +14 authors to writing the manuscript. Additional information Com interests
  • Reprints and permission information is available online at http://npg.nature.com/ reprintsandpermissions/ How to cite this article: Wilding, T. J. et al. Radial symmetry in a chimeric glutamate receptor pore. Nat. Commun. 5:3349 doi: 10.1038/ncomms4349
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