Figure 2.

Structure graphic of AMPK. The α subunit is in red, the β subunit in green, and the four CBS motifs of the γ subunit in various shades of blue, magenta and cyan. For this structure, an AMPK complex phosphorylated on Thr172, lacking most of the β subunit and also a flexible loop from the α subunit, was crystallized in the presence of AMP and the kinase inhibitor staurosporine. For clarity, only the AMP in site 3 is shown, but the approximate location of binding clefts 1, 2 and 4 are also shown; in this view, sites 1 and 4 are at the back of the γ subunit and sites 2 and 3 at the front. The carboxy-terminal domain of the β subunit forms the core of the complex, bridging the carboxy-terminal domain of the α subunit and the γ subunit. Note the extended α subunit linker peptide between the kinase domain and carboxy-terminal domain, with its 'α hook' region contacting AMP in site 3. AID: α subunit autoinhibitory domain (this domain is believed to hold the catalytic domain in an inactive conformation in the absence of the regulatory domains). Drawn using MacPyMOL with Protein Database Entry 2Y94 [15].

Hardie and Alessi BMC Biology 2013 11:36   doi:10.1186/1741-7007-11-36
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