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. Author manuscript; available in PMC: 2017 Dec 12.
Published in final edited form as: Nat Rev Mol Cell Biol. 2012 Mar 22;13(4):251–262. doi: 10.1038/nrm3311

Figure 2.

Figure 2

Domain map of typical mammalian AMPK. Colour coding of domains are similar to those in Figs. 1 and 3. AMPK complexes are heterotrimers composed of α, β and γ subunits in a 1:1:1 ratio. Key to acronyms: N-lobe, N-terminal lobe of kinase domain; C-lobe, C-terminal lobe of kinase domain; AID, auto-inhibitory domain; α-CTD, α subunit C-terminal domain; CBM, carbohydrate-binding module; β-CTD, β subunit C-terminal domain; CBS1-4, CBS repeats in γ subunit. The β-CTD forms the core of the complex, binding to the α-CTD and the N-terminus of the γ subunit prior to CBS1.