Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies-Reference-Cited by-同舟云学术

Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies

Published:2019-04-17 Issue:1 Volume:9 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Renart M. Lourdes^ORCID,Giudici A. Marcela,Poveda José A.,Fedorov Aleksander,Berberan-Santos Mário N.,Prieto Manuel,Díaz-García Clara,González-Ros José M.,Coutinho Ana

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-019-42405-5.pdf

Reference50 articles.

1. Hille, B. Ion Channels of Excitable Membranes. 3rd, (Sinauer Associates, Inc. 2001).

2. Doyle, D. A. et al. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Sci. 280, 69–77 (1998).

3. Zhou, Y., Morais-Cabral, J. H., Kaufman, A. & MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nat. 414, 43–48 (2001).

4. Ostmeyer, J., Chakrapani, S., Pan, A. C., Perozo, E. & Roux, B. Recovery from slow inactivation in K+ channels is controlled by water molecules. Nature 501 (2013).

5. Blunck, R., Cordero-Morales, J. F., Cuello, L. G., Perozo, E. & Bezanilla, F. Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction. J. Gen. Physiol 128, 569–581 (2006).

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