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JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
1 H, 13 C and 15 N backbone and side-chain resonance assignments of the ZnF-UBP domain of USP20/VDU2.
Biomolecular NMR Assignments 2017 April
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 1 H, 13 C and 15 N 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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