Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression.

@article{BaileyElkin2014CrystalSO,
  title={Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression.},
  author={Ben A Bailey-Elkin and Robert C M Knaap and Garrett G R J Johnson and Tim J Dalebout and Dennis K. Ninaber and Puck van Kasteren and Peter J. Bredenbeek and Eric J. Snijder and Marjolein Kikkert and Brian L. Mark},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 50},
  pages={34667-82}
}
Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly emerging human pathogen that was first isolated in 2012. MERS-CoV replication depends in part on a virus-encoded papain-like protease (PL(pro)) that cleaves the viral replicase polyproteins at three sites releasing non-structural protein 1 (nsp1), nsp2, and nsp3. In addition to this… CONTINUE READING