Destabilization Domains (DDs)

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  • Published date: March 29, 2019
  • Modified date: October 17, 2019
    • Shirley, New York, United States

Designing small-molecule ligands for a protein can be challenging and time-consuming as the process usually involves multiple rounds of screening and structural modification. Thus, it is beneficial to have a hybrid system that takes advantage of the simplicity of small-molecule ligands and the specificity of genetic approaches. Destabilization domains (DDs) represent a fusion protein component that is intrinsically unstable and destabilizes other proteins upon incorporation, leading to protein degradation. A well-known example of DDs is the Shield system, which incorporated a rampamycin-binding protein (FKBP12) into proteins as a build-in destabilizing domain to cause protein degradation in cells (Figure 1). However, when a rampamycin analogue (Shield1) is added to bind the destabilizing domain, the fusion protein can be stabilized and returns expression to a normal level. This approach enables the regulation of secreted proteins and their biological activity, which opens up new avenues for various applications such as cancer therapy and targeted gene delivery.

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Anna Camp
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