Crystal structure of the tetramerization domain of the Shaker potassium channel

Article Abstract:

The crystal structure of the T1 domain of a Shaker potassium channel has been determined at 1.55 A resolution. Four identical subunits are revealed, arranged in a four-fold symmetry around a centrally located pore of around 20A in length. The majority of highly conserve amino acids in the T1 domain of potassium channels are located in the core of the protein, suggesting a common structural tetramer assembly framework.

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Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel

Article Abstract:

Fluorescence resonance energy transfer has been used as a spectroscopic ruler to establish distances between S4s in the Shaker K+ channel in different gating states. It has been possible to produce evidence indicating that S4 is a tilted helix that twists during activation. It appears that the transmission of S4 twist to the pore domain may link voltage sensor motion with the opening of the internal mouth of the pore.

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Cell-free expression of functional Shaker potassium channels

Article Abstract:

Protein expression and modulation processes can be subjected to greater experimental control through the use of a cell-free method of ion channel expression. Such a method is demonstrated in the manipulation and observation of Shaker potassium channels. Ion channel expression had required the use of target cells such as Xenopus oocytes, but this complicated the interpretation of results.

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