期刊
PLOS ONE
卷 10, 期 1, 页码 -出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0115344
关键词
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资金
- Biomedical Research Centre, Oxford, UK
- Swedish Medical Research Council
- StratNeuro
- foundation of Ake Wiberg
- foundation of Jeanssons
- foundation of Ahlen
- foundation of Magnus Bergvalls
- foundation of Wenner-Gren
- Medical Research Council [G1000099, G0501068, G1100525, MR/N00065X/1] Funding Source: researchfish
- MRC [MR/N00065X/1, G0501068, G1000099] Funding Source: UKRI
Ovarian tumor domain containing proteases cleave ubiquitin (Ub) and ubiquitin-like polypeptides from proteins. Here we report the crystal structure of human otubain 2 (OTUB2) in complex with a ubiquitin-based covalent inhibitor, Ub-Br2. The ubiquitin binding mode is oriented differently to how viral otubains (vOTUs) bind ubiquitin/ISG15, and more similar to yeast and mammalian OTUs. In contrast to OTUB1 which has exclusive specificity towards Lys48 poly-ubiquitin chains, OTUB2 cleaves different poly-Ub linked chains. N-terminal tail swapping experiments between OTUB1 and OTUB2 revealed how the N-terminal structural motifs in OTUB1 contribute to modulating enzyme activity and Ub-chain selectivity, a trait not observed in OTUB2, supporting the notion that OTUB2 may affect a different spectrum of substrates in Ub-dependent pathways.
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