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PDBsum entry 5k7l
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Metal transport/calcium binding protein
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PDB id
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5k7l
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References listed in PDB file
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Key reference
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Title
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Structure of the voltage-Gated k⁺ channel eag1 reveals an alternative voltage sensing mechanism.
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Authors
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J.R.Whicher,
R.Mackinnon.
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Ref.
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Science, 2016,
353,
664-669.
[DOI no: ]
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PubMed id
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Abstract
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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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