Abstract
Deubiquitinase USP20/VDU2 has been identified as a regulator of multiple proteins including hypoxia-inducible factor (HIF)-1α, β2-adrenergic receptor, and tumor necrosis factor receptor associated factor 6 etc. It contains four structural domains, including an N-terminal zinc-finger ubiquitin binding domain (ZnF-UBP) that potentially helps USP20 to recruit its ubiquitin substrates. Here we report the 1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF-UBP domain of USP20/VDU2. The BMRB accession number is 26901. The secondary structural elements predicted from the NMR data reveal a global fold consisting of three α-helices and four β-strands. The complete assignments can be used to explore the protein dynamics of the USP20 ZnF-UBP and its interactions with monoubiquitin and ubiquitin chains.
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This work was funded by the National Natural Science Foundation of China (Grant Numbers 21272246 to N. Z. and 31300608 to Y. W.) and the National Key Basic Research Program of China (Grant Number 2013CB910900 to N. Z.).
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Yang, Y., Wen, Y. & Zhang, N. 1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF-UBP domain of USP20/VDU2. Biomol NMR Assign 11, 91–93 (2017). https://doi.org/10.1007/s12104-017-9726-y
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DOI: https://doi.org/10.1007/s12104-017-9726-y