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This study investigates the biochemical mechanisms underlying the activation of Gal4-CycT1 and its interaction with HEXIM1 proteins. By examining the conserved domains and the specific residues involved in these interactions, we aim to deepen our understanding of transcription regulation in cellular processes. A detailed analysis of the activation folds and the impact of various mutations on GAL4 and HEXIM1 function is presented. This research could provide insights into potential therapeutic targets for diseases associated with transcription dysregulation.
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A B 20 20 16 16 12 12 Fold Activation Fold Activation 8 8 4 4 1 2 3 4 5 6 7 8 9 10 11 1 2 3 4 5 6 7 8 9 10 11 Tat + + + + + + + + + + - + + + + + + + + + + Gal4-CycT1 wt PYND ILAA wt PYND ILAA HEXIM1 HEXIM1 wt ILAA PYND F:HEXIM1 HEXIM1 cyclinT1 Basic Domain Conserved domain 359 1 HEXIM1 152-KHRR-155 ILAA 202-PYNT-205 PYND C