Abstract
To compare the stimulation and binding characteristics of adenosine analogs including AMP, IMM-H007, and M1, to AMPK, and to explore the potential mechanism underlying the regulation effect of adenosine analogs on AMPK activity, [γ-32P]ATP assay, circular dichroism experiments and molecular docking test were performed. We found that the interactions with Thr86, Thr88, and His150 in site 1 are probably the reason why the affinities of IMM-H007, M1, and adenosine are comparable but their allosteric activation on AMPK varies greatly, partly interpreting the mechanism of AMPK activity regulated by adenosine analogs.
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