Article
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.
The Journal of biological chemistry - 12 Dec 2014
Bailey-Elkin Ben A, Knaap Robert C M, Johnson Garrett G, Dalebout Tim J, Ninaber Dennis K, van Kasteren Puck B, Bredenbeek Peter J, Snijder Eric J, Kikkert Marjolein, Mark Brian L
Abstract excerpt
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 replicative function, MERS-CoV PL(pro) was recently shown to be a...
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