Huang, Q., Ng, H. Q., & Kang, C. (2026). Backbone resonance assignment of the Thalidomide Binding Domain (TBD) of cereblon. Biomolecular NMR Assignments, 20(1). https://doi.org/10.1007/s12104-026-10266-5
Abstract:
Cereblon is a key E3 ubiquitin ligase that plays a central role in protein ubiquitination through its cooperation with other components of the ubiquitin–proteasome system. With the emergence of PROteolysis TArgeting Chimera (PROTAC) technology as a powerful strategy for inducing selective protein degradation, cereblon has become a highly attractive target in drug discovery. Although PROTAC-mediated degradation involves the assembly of a multi-protein complex, the Thalidomide-Binding Domain (TBD) of cereblon plays important roles in recruiting PROTAC molecules. In this study, we purified the human cereblon TBD for NMR studies and herein report its backbone resonance assignments. The purified TBD was shown to interact with the cereblon ligand lenalidomide, confirming its functional integrity. These resonance assignments provide a valuable foundation for characterizing ligand binding and for evaluating and optimizing small molecules targeting the cereblon TBD in targeted protein degradation strategies.
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Publisher Copyright
Funding Info:
This research is supported by core funding from: Experimental Drug Development Centre (EDDC)
Grant Reference no. : Core
Description:
This is a post-peer-review, pre-copyedit version of an article published in Biomolecular NMR Assignments. The final authenticated version is available online at: http://dx.doi.org/10.1007/s12104-026-10266-5.