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. Author manuscript; available in PMC: 2018 Mar 4.
Published in final edited form as: EXS. 2016;107:389–401. doi: 10.1007/978-3-319-43589-3_16

Fig. 16.1. Conservation of carboxy-terminus residues in AMPK-β.

Fig. 16.1

Most amino acids in the C-terminus of human AMPK-β1 (NM_006253.4), rat AMPK-β1 (GenBank: X95577.1), and Drosophila AMPK-β (NP_995783.1) are either invariant (gray) or have residues with conserved hydrophilicity (green) or hydrophobicity (yellow). Amino acids 246–270 (underlined) in rAMPK-β1 are required for binding to AMPK-γ; amino acids 186–270 in rAMPK-β1 are required for heterotrimer formation (Iseli et al. 2005)