File:Structure of full-length AMPK complex with activator Fig3c.jpg
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Summary
| Description |
English: "Structure of full-length AMPK complex with activator: Detailed view of 991 binding in a pocket generated at the interface between the CBM and the kinase domain, and making interactions with a cluster of hydrophobic residues from each domain; Ile-46(Kinase), Phe-90(Kinase), Leu-18(Kinase) and Val-11(Kinase) and Val-81(CBM), Val-113(CBM), Ile-115(CBM) and one of the side-chain carbon atoms (CG) of Thr-106(CBM). These hydrophobic interactions mainly involve ring-1 and ring-2 of the activator. The hydrophobic residues from the kinase (yellow) and CBM (green) are shown as sticks with surfaces." Figure 3c from B.Xiao et al. "Structural basis of AMPK regulation by small molecule activators" Nature Communications 4 doi:10.1038/ncomms4017 . Image and description copied under CC-BY 3.0 licence. |
| Date | |
| Source | http://www.nature.com/ncomms/2013/131219/ncomms4017/fig_tab/ncomms4017_F3.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 |
| Permission (Reusing this file) |
doi:10.1038/ncomms4017 |
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doi:10.1038/ncomms4017, was reviewed on 5 February 2015 by reviewer Yann, who confirmed that it was available there under the stated license on that date.
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 15:26, 14 November 2014 | | 375 × 289 (31 KB) | MartinPoulter | User created page with UploadWizard |
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