DescriptionThe structure of the alpha2 hook of AMPK Fig 4b.jpg
English: "Detailed view of the α2 hook (coloured in orange with the residue carbons in yellow) and its interaction with residues at the AMP-3 site on the γ-subunit (coloured pink with the residue carbons in grey) and with a loop from the β-subunit (coloured green with the carbons in grey). AMP-3 is shown in stick representation (with the carbons coloured in grey). His-366(α2-hook) forms a salt bridge with Glu-296(γ), while the following proline at position 367 introduces a kink into the chain, which seems instrumental in positioning Glu-368(α2-hook) that makes salt-bridges to Lys-170(γ) and Arg-70(γ). Arg-369(α2-hook) makes hydrogen bonds with three residues on a loop from the β-subunit, Thr-219(β), and the main-chain carbonyl oxygen of Gly-220(β). Potential interactions are indicated by a thin dashed blue line." Figure 4b from B.Xiao et al. "Structural basis of AMPK regulation by small molecule activators" Nature Communications4doi:10.1038/ncomms4017 . Image and description copied under CC-BY 3.0 licence.
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
to share – to copy, distribute and transmit the work
to remix – to adapt the work
Under the following conditions:
attribution – You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
https://creativecommons.org/licenses/by/3.0CC BY 3.0 Creative Commons Attribution 3.0 truetrue
Captions
Add a one-line explanation of what this file represents