Structural basis for AMP binding to mammalian AMP-activated protein kinase

By B. Xiao, R. Heath, P. Saiu, F. C. Leiper, P. Leone, C. Jing, P. Walker, L. Haire, J. Eccleston, C. Davis and 3 more. Nature, 2007

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Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation (2010, background): “This is consistent with structural studies of g1 showing that the side chain of Arg-298 (equivalent to Arg-531 in g2) is directly involved in binding of AMP and ATP to the exchangeable site formed by CBS repeats 3 and 4 (Xiao et al., 2007).”
AMPK - a nutrient and energy sensor that maintains energy homeostasis (2012, neutral): “, and they have variable occupancies in the crystal structures of partial complexes from mammals and fung”
AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. (2011, background): “These assemble in a pseudosymmetrical manner, such that there are four clefts where adenine nucleotides might bind (Scott et al. 2004; Xiao et al. 2007, 2011).”