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• W2797291909 endingPage "1792" @default.
• W2797291909 startingPage "1783" @default.
• W2797291909 abstract "Deregulated kinase activity of anaplastic lymphoma kinase (ALK) has been observed to be implicated in the development of tumor progression. The activation mechanism of ALK is proposed to be similar to other receptor tyrosine kinases (RTKs), but the distinct static X-ray crystal conformation of ALK suggests its unique conformational transition. Herein, we have illustrated the dynamic conformational property of wild-type ALK as well as the kinase activation equilibrium variation induced by two neuroblastoma mutations (R1275Q and Y1278S) and ATP binding by performing enhanced sampling accelerated Molecular Dynamics (aMD) simulations. The results suggest that the wild-type ALK is mostly favored in the inactive state, whereas the mutations and ATP binding promote a clear shift toward the active-like conformation. The R1275Q mutant stabilizes the active conformation by rigidifying the αC-in conformation. The Y1278S mutant promotes activation at the expense of a π-stacking hydrophobic cluster, which plays a critical role in the stabilization of the inactive conformation of native ALK. ATP produces a more compact active site and thereby facilitates the activation of ALK. Taken together, these findings not only elucidate the diverse conformations in different ALKs but can also shed light on new strategies for protein engineering and structural-based drug design for ALK." @default.
• W2797291909 created "2018-04-24" @default.
• W2797291909 creator A5009654446 @default.
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• W2797291909 date "2018-04-11" @default.
• W2797291909 modified "2023-10-18" @default.
• W2797291909 title "Conformational Transition of Key Structural Features Involved in Activation of ALK Induced by Two Neuroblastoma Mutations and ATP Binding: Insight from Accelerated Molecular Dynamics Simulations" @default.
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• W2797291909 doi "https://doi.org/10.1021/acschemneuro.8b00105" @default.
• W2797291909 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29638111" @default.
• W2797291909 hasPublicationYear "2018" @default.
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