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After simulations, we discovered the conformational space of apo APC and identified its two major conformers. Then, the conformation selection mechanism was unraveled by the free energy landscapes of APC-ligands. Analyses based on representative structures explain the reason why MAI-108 fits ligand-competent M1, but Asef and ΔAsef fit ligand-incompetent M2. In stability analysis, we found that APC stability is positively related to inhibitor efficiency and confirms the structural analyses. Hence, increasing the ability to maintain APC stability, especially in the interface, contributes to the optimization of inhibitors. Next, DCCM unveils the dynamic properties of systems, suggesting a different ability of ligands to control the movement of APC residues. This ability tends to provide a binding affinity. At last, binding energy analysis based on MM/GBSA quantitatively identifies important residues for binding and guide future optimization. In total, our simulations explain the mechanism of the inhibitor and provide insights for lead compound design from a perspective of protein dynamics. 2ff7e9595c
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