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.
https://www.profacgen.com/Destabilization-Domains-DDs.htm

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