Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.

@article{Clayton2009CrystalSO,
  title={Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.},
  author={Amber J. Clayton and Christian Siebold and Robert J C Gilbert and Geoffrey C. Sutton and Karl Harlos and Robert Andrew Jeffrey Mcilhinney and Edith Yvonne Jones and A. Radu Aricescu},
  journal={Journal of molecular biology},
  year={2009},
  volume={392 5},
  pages={
          1125-32
        }
}
Ionotropic glutamate receptors are functionally diverse but have a common architecture, including the 400-residue amino-terminal domain (ATD). We report a 1.8-A resolution crystal structure of human GluR2-ATD. This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. Lattice contacts in a 4.1-A resolution crystal form reveal a tetrameric (dimer-dimer) arrangement consistent with previous cellular and cryo-electron microscopic… CONTINUE READING
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