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Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels
Comparison of the crystal structures of the KcsA and MthK potassium channels suggests that the process of opening a K(+) channel involves pivoted bending of the inner pore-lining helices at a highly conserved glycine residue. This bending motion is proposed to splay the transmembrane domains outward...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Springer-Verlag
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190780/ https://www.ncbi.nlm.nih.gov/pubmed/17657484 http://dx.doi.org/10.1007/s00249-007-0206-7 |