• adenosine monophosphate (AMP);
  • AMP-activated protein kinase;
  • cordycepin;
  • cordycepin monophosphate;
  • molecular docking

It had been reported that cordycepin could activate AMP-activated protein kinase. One possible mechanism is that cordycepin mediated AMP-activated protein kinase activation by conversion into cordycepin monophosphate, which acts as an AMP analog to activate AMP-activated protein kinase. To confirm the aforementioned hypothesis, we investigate the binding of cordycepin monophosphate to AMP-activated protein kinase using molecular docking. The modeling results indicate that cordycepin monophosphate binds to AMP-activated protein kinase with high affinity. The hydrogen bonds provide attractive forces between molecules. Our results further identify the key residues contributing to the interaction. Also, the modeling results predict that cordycepin monophosphate and AMP would have similar binding modes with AMP-activated protein kinase. Further investigation of AMP-activated protein kinase activation in vitro provides the evidence that cordycepin monophosphate functioned as an AMP mimic to activate AMP-activated protein kinase.