Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing
Journal
Nature Communications
Publication Date
2012
Volume
3
Inclusive Pages
1102
Document Type
Open Access Publication
DOI
10.1038/ncomms2077
Rights and Permissions
E.C. McCusker, et al. 02 October 2012. Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing. Nature communications. Art. No. 1102. DOI: 10.1038/ncomms2077. http://www.nature.com/ncomms/journal/v3/n10/full/ncomms2077.html
Recommended Citation
McCusker, Emily C.; Bagnéris, Claire; Naylor, Claire E.; Cole, Ambrose R.; D'Avanzo, Nazzareno; Nichols, Colin G.; and Wallace, B A., "Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing." Nature Communications. 3, 1102. (2012).
https://digitalcommons.wustl.edu/open_access_pubs/4331
Supplementary Figures S1-S6
ncomms2077-s3.mpg (931 kB)
Movie showing the morphing between open and closed pore structures. The four monomers are depicted in different colours. View from the intracellular surface.
ncomms2077-s4.mpg (634 kB)