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Upon binding, Asp1116 assumed a conformation that altered the architecture of the bromodomain active site, thereby orienting the helices around the active site in a more compacted position. Interestingly, in addition to some specific structural perturbations mediated by Asp1116 on the dynamics of CBP, our study revealed that the strong hydrogen bond interaction (N-H⋯O) elicited in CBP-Y08197 sequestered Y08197 tightly into the CBP bromodomain active site. CONCLUSION Conclusively, the inhibition and selective pattern of Y08197 can be replic
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