Structural basis for the cAMP-dependent gating in the human HCN4 channel.

@article{Xu2010StructuralBF,
  title={Structural basis for the cAMP-dependent gating in the human HCN4 channel.},
  author={Xinping Xu and Zhanna V. Vysotskaya and Qinglian Liu and Lei Zhou},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 47},
  pages={37082-91}
}
Hyperpolarization-activated cAMP-regulated (HCN) channels play important physiological roles in both cardiovascular and central nervous systems. Among the four HCN isoforms, HCN2 and HCN4 show high expression levels in the human heart, with HCN4 being the major cardiac isoform. The previously published crystal structure of the mouse HCN2 (mHCN2) C-terminal fragment, including the C-linker and the cyclic-nucleotide binding domain (CNBD), has provided many insights into cAMP-dependent gating in… CONTINUE READING
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