Abstract
Ubiquitin-conjugating enzyme E2 T (UBE2T) plays important roles in ubiquitination of proteins through participation in transferring ubiquitin to its substrate. Due to its importance in protein modifications, UBE2T associates with diverse diseases and serves as an important target for drug discovery and development. The crystal structure of UBE2T has been determined and the structure reveals the lack of a druggable pocket for binding to small molecules for clinical applications. Despite the challenge, effort has been made to develop UBE2T inhibitors. We obtained UBE2T constructs with and without the C-terminal region which is flexible in solution. Herein, we report the backbone resonance assignments for human UBE2T without the C-terminal region. The backbone dynamics of UBE2T was also explored. The available assignments will be helpful for hit identification, determining ligand binding site and understanding the mechanism of action of UBE2T inhibitors.
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Data availability
The assignments have been deposited to the BMRB under the accession code: 52,051.
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Authors appreciate the useful discussion with colleagues at EDDC.
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Q.H. and H.Q.N. carried out protein purification. Y.Y.L., Z.K., W.H. L. and C.K. designed the experiments. C.K. analysed data and drafted the manuscript. All authors approved the manuscript.
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Huang, Q., Ng, H.Q., Loh, Y.Y. et al. Backbone 1H, 15N and 13C resonance assignments for an E2 ubiquitin conjugating enzyme-UBE2T. Biomol NMR Assign 17, 269–274 (2023). https://doi.org/10.1007/s12104-023-10154-2
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DOI: https://doi.org/10.1007/s12104-023-10154-2