File:Structure of full-length AMPK complex with activator Fig3b.jpg
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[edit]DescriptionStructure of full-length AMPK complex with activator Fig3b.jpg |
English: Structure of full-length AMPK complex with activator: Cartoon representation of full-length α2β1γ1 in complex with the activator 991, the domains of the three subunits are coloured according to the bar chart File:Structure_of_full-length_AMPK_complex_with_activator_Fig3a.gif. The orientation of the figure is such that the kinase domain is ‘upside-down’ with respect to the classical kinase orientation. The activator, which binds at the interface of the kinase and CBM, is shown in stick representation with its carbon atoms coloured magenta. Omit density (Fo-Fc) covering the 991 compound is contoured at 2.5 sigma and coloured blue. Figure 3b from B.Xiao et al. "Structural basis of AMPK regulation by small molecule activators" Nature Communications 4 doi:10.1038/ncomms4017 . Image and description adapted under CC-BY 3.0 licence. |
Date | |
Source | http://www.nature.com/ncomms/2013/131219/ncomms4017/full/ncomms4017.html |
Author | Bing Xiao, Matthew J. Sanders, David Carmena, Nicola J. Bright, Lesley F. Haire, Elizabeth Underwood, Bhakti R. Patel, Richard B. Heath, Philip A. Walker, Stefan Hallen, Fabrizio Giordanetto, Stephen R. Martin, David Carling & Steven J. Gamblin |
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