Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease.

@article{Bks2016RecognitionOL,
  title={Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease.},
  author={Mikl{\'o}s B{\'e}k{\'e}s and Gerbrand J van der Heden van Noort and Reggy Ekkebus and Huib Ovaa and Tony T Huang and Christopher D Lima},
  journal={Molecular cell},
  year={2016},
  volume={62 4},
  pages={572-85}
}
Deubiquitinating enzymes (DUBs) recognize and cleave linkage-specific polyubiquitin (polyUb) chains, but mechanisms underlying specificity remain elusive in many cases. The severe acute respiratory syndrome (SARS) coronavirus papain-like protease (PLpro) is a DUB that cleaves ISG15, a two-domain Ub-like protein, and Lys48-linked polyUb chains, releasing diUb(Lys48) products. To elucidate this specificity, we report the 2.85 Å crystal structure of SARS PLpro bound to a diUb(Lys48) activity-based… CONTINUE READING
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