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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...

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Autori principali: Shang, Lijun, Tucker, Stephen J.
Natura: Artigo
Lingua:Inglês
Pubblicazione: Springer-Verlag 2007
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2190780/
https://ncbi.nlm.nih.gov/pubmed/17657484
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s00249-007-0206-7
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