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The TAZ1 domain of CREB binding protein is crucial for transcriptionalregulation and recognizes multiple targets. The interactions between TAZ1 andits specific targets are related to the cellular hypoxic negative feedbackregulation. Previous experiments reported that one of the TAZ1 targets CITED2is an efficient competitor of another target HIF-1{\alpha}. Here by developingthe structure-based models of TAZ1 complexes we have uncovered the underlyingmechanisms of the competitions between HIF-1{\alpha} and CITED2 binding toTAZ1. Our results are consistent with the experimental hypothesis on thecompetition mechanisms and the apparent affinity. In addition, the simulationsprove the dominant position of forming TAZ1-CITED2 complex in boththermodynamics and kinetics. For thermodynamics, TAZ1-CITED2 is the lowestbasin located on the free energy surface of binding in the ternary system. Forkinetics, the results suggest that CITED2 binds to TAZ1 faster thanHIF-1{\alpha}. Besides, the analysis of contact map and f values in this studywill be helpful for further experiments on TAZ1 systems.

Investigations of the Underlying Mechanisms of HIF-1{\alpha} and CITED2 Binding to TAZ1