Binding Symmetry of External Divalent Cations to Cyclic Nucleotide-gated IonChannel Reveled by Channel Tandem Dimers

  • Kwon, Ryuk-Jun (Laboratory of Molecular Neurobiology, Department of Life Science, Kwangju Institute of Science and Technology) ;
  • Park, Chul-Seung (Laboratory of Molecular Neurobiology, Department of Life Science, Kwangju Institute of Science and Technology)
  • Published : 2001.06.01

Abstract

Cyclic nucleotide-gated (CNG) channels are composed of homo or hetero tetramer of ${\alpha}$ and ${\beta}$ subunits. The a subunits of these channels have a conserved glutamate residue within the pore-forming region. This residue determines the selectivity as well as the affinity for the extracellular divalent cations. Using the high affinity mutant (E363D) of bovine retinal CNG channel in which the Glu was replaced to Asp at position 363, we constructed tandem dimers and investigated the binding symmetry of divalent cation to the site.(omitted)

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