Tetramerization dynamics of C-terminal domain underlies isoform-specific cAMP gating in hyperpolarization-activated cyclic nucleotide-gated channels.

@article{Lolicato2011TetramerizationDO,
  title={Tetramerization dynamics of C-terminal domain underlies isoform-specific cAMP gating in hyperpolarization-activated cyclic nucleotide-gated channels.},
  author={Marco Lolicato and Marco Nardini and Sabrina Gazzarrini and Stefan Moeller and Daniela Bertinetti and Friedrich W Herberg and Martino Bolognesi and Holger Martin and Marina Fasolini and Jay A. Bertrand and Cristina Arrigoni and Gerhard Thiel and Anna Moroni},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 52},
  pages={44811-20}
}
Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels are dually activated by hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD). HCN isoforms respond differently to cAMP; binding of cAMP shifts activation of HCN2 and HCN4 by 17 mV but shifts that of HCN1 by only 2-4 mV. To explain the peculiarity of HCN1, we solved the crystal structures and performed a biochemical-biophysical characterization of the C-terminal domain (C-linker plus CNBD) of the… CONTINUE READING

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