Journal
SCIENCE
Volume 353, Issue 6300, Pages 664-669Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf8070
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Funding
- NIH [GM43949]
- Damon Runyon Cancer Research Foundation [DRG-2212-15]
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Voltage-gated potassium (K-v) channels are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4-S5 linker, to the potassium pore. We determined the single-particle cryo-electron microscopy structure of mammalian K(v)10.1, or Eag1, bound to the channel inhibitor calmodulin, at 3.78 angstrom resolution. Unlike previous K-v structures, the S4-S5 linker of Eag1 is a five-residue loop and the transmembrane segments are not domain swapped, which suggest an alternative mechanism of voltage-dependent gating. Additionally, the structure and position of the S4-S5 linker allow calmodulin to bind to the intracellular domains and to close the potassium pore, independent of voltage-sensor position. The structure reveals an alternative gating mechanism for K-v channels and provides a template to further understand the gating properties of Eag1 and related channels.
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