期刊
PROTEIN SCIENCE
卷 16, 期 9, 页码 2072-2075出版社
WILEY
DOI: 10.1110/ps.072967807
关键词
VHL; deubiquitination; HDAC6; IMP
资金
- Medical Research Council [MC_U105459896] Funding Source: Medline
- Medical Research Council [MC_U105459896] Funding Source: researchfish
- MRC [MC_U105459896] Funding Source: UKRI
USP33/VDU1 is a deubiquitinating enzyme that binds to the von Hippel-Lindau tumor suppressor protein. It also regulates thyroid hormone activation by deubiquitinating type 2 iodothyronine deiodinase. USP33/VDU1 contains a ZF UBP domain, a protein module found in many proteins in the ubiquitin proteasome system. Several ZF UBP domains have been shown to bind ubiquitin, and a structure of a complex of the ZF UBP domain of isoT/USP5 and ubiquitin is available. In the present work, the solution structure of the ZF UBP domain of USP33/VDU1 has been determined by NMR spectroscopy. The structure differs from that of the USP5 domain, which contains only one of the three Zn ions present in the USP33/VDU1 structure. The USP33/VDU1 ZnF UBP domain does not bind to ubiquitin.
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