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Crystal structure of full-length KcsA in its closed conformation
KcsA is a proton-activated, voltage-modulated K(+) channel that has served as the archetype pore domain in the Kv channel superfamily. Here, we have used synthetic antigen-binding fragments (Fabs) as crystallographic chaperones to determine the structure of full-length KcsA at 3.8 Å, as well as that...
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| Main Authors: | , , , , , , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
National Academy of Sciences
2009
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| Teme: | |
| Online dostop: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2672561/ https://ncbi.nlm.nih.gov/pubmed/19346472 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0810663106 |
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