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Metadynamics simulation of the DFG conformational transition in calmodulin kinase II
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DOI：10.1016/j.cplett.2026.142768.png)
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Abstract
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We performed metadynamics simulations based on the DFGin conformation of CaMKII alpha to obtain its DFGout conformation. Based on the enhanced sampling results, we constructed the free energy landscape of the DFG conformational change of CaMKII alpha and analyzed the pathway of it. Through analysis, we revealed the flipping direction of residues in the DFG and analyzed the effect of DFG flipping on the size of the ATP-binding pocket and surrounding hydrogen bonding. This study provides a theoretical basis for the design and molecular docking of inhibitory drugs targeting CaMKII.
Keywords:
DFG-motif
CaMKII kinase
Conformational change
Metadynamics
MD simulation
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