These two authors contributed equally to this work.
Research Article: Binding of Cordycepin Monophosphate to AMP-Activated Protein Kinase and its Effect on AMP-Activated Protein Kinase Activation
Version of Record online: 3 AUG 2010
© 2010 John Wiley & Sons A/S
Chemical Biology & Drug Design
Volume 76, Issue 4, pages 340–344, October 2010
How to Cite
Wang, Z., Wang, X., Qu, K., Zhu, P., Guo, N., Zhang, R., Abliz, Z., Yu, H. and Zhu, H. (2010), Research Article: Binding of Cordycepin Monophosphate to AMP-Activated Protein Kinase and its Effect on AMP-Activated Protein Kinase Activation. Chemical Biology & Drug Design, 76: 340–344. doi: 10.1111/j.1747-0285.2010.01019.x
- Issue online: 6 SEP 2010
- Version of Record online: 3 AUG 2010
- Received 24 November 2009, revised 25 June 2010 and accepted for publication 3 July 2010
- adenosine monophosphate (AMP);
- AMP-activated protein kinase;
- 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.