Membrane anchoring and interaction between transmembrane domains are crucial for K+ channel function.

@article{Gebhardt2011MembraneAA,
  title={Membrane anchoring and interaction between transmembrane domains are crucial for K+ channel function.},
  author={Manuela M Gebhardt and Franziska Hoffgaard and Kay Hamacher and Stefan M. Kast and Antoni Moroni and Gerhard Thiel},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 13},
  pages={
          11299-306
        }
}
The small viral channel Kcv is a Kir-like K(+) channel of only 94 amino acids. With this simple structure, the tetramer of Kcv represents the pore module of all complex K(+) channels. To examine the structural contribution of the transmembrane domains (TMDs) to channel function, we performed Ala scanning mutagenesis of the two domains and tested the functionality of the mutants in a yeast complementation assay. The data reveal, in combination with computational models, that the upper halves of… CONTINUE READING
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