IPR043178
Papain-like protease, thumb domain superfamily, coronavirus
InterPro entry
Short name | PLpro_thumb_sf_CoV |
Overlapping entries |
Description
All coronaviruses such as the SARS virus and the Middle East Respiratory Syndrome (MERS) virus encode in their genomes at least one papain-like protease (PLpro) enzyme which cleaves the viral replicase polyproteins at three sites releasing non-structural protein NSP1, NSP2 and NSP3. PLpro also possesses deubiquitinating and deISGylating activities. These have been suggested to suppress the host antiviral response by counteracting the post-translational modification of signalling molecules that activate the innate immune response. PLpro is made up of an N-terminal ubiquitin-like domain (found in many ubiquitin-specific proteases or USPs) and a C-terminal catalytic domain containing a right-handed fingers, palm, and thumb domain organisation
[2, 1, 3, 4].
References
1.Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating activity of SARS-CoV papain-like protease. Ratia K, Kilianski A, Baez-Santos YM, Baker SC, Mesecar A. PLoS Pathog. 10, e1004113, (2014). PMID: 24854014
2.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. Bailey-Elkin BA, Knaap RC, Johnson GG, Dalebout TJ, Ninaber DK, van Kasteren PB, Bredenbeek PJ, Snijder EJ, Kikkert M, Mark BL. J. Biol. Chem. 289, 34667-82, (2014). PMID: 25320088
Cross References
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:1.10.8.1190