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Mechanism of activation gating in the full-length KcsA K(+) channel
Using a constitutively active channel mutant, we solved the structure of full-length KcsA in the open conformation at 3.9 Å. The structure reveals that the activation gate expands about 20 Å, exerting a strain on the bulge helices in the C-terminal domain and generating side windows large enough to...
Αποθηκεύτηκε σε:
| Κύριοι συγγραφείς: | , , , , , |
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| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
National Academy of Sciences
2011
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3141920/ https://ncbi.nlm.nih.gov/pubmed/21730186 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1105112108 |
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