SARS-CoV-2 enzyme Papain-like: Difference between revisions
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<SX viewer='molstar' load='6w9c' size='340' side='right' caption='The crystal structure of papain-like protease of SARS CoV-2 (PDB: | <SX viewer='molstar' load='6w9c' size='340' side='right' caption='The crystal structure of papain-like protease of SARS CoV-2 (PDB: 6w9c).' scene=''> | ||
'''Papain-like proteinase''' | '''Papain-like proteinase''' | ||
Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.<ref>[https://zhanglab.ccmb.med.umich.edu/COVID-19/ Modeling of the SARS-COV-2 Genome]</ref><ref>pmid 32200634</ref> | Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.<ref>[https://zhanglab.ccmb.med.umich.edu/COVID-19/ Modeling of the SARS-COV-2 Genome]</ref><ref>pmid 32200634</ref> | ||
==Function & Structure == | ==Function & Structure of the Non-structural Protein 3 == | ||
The SARS-CoV-2 non-structural protein nsp3 contains 1945 amino acids and is therefore the largest of the viruses proteins<ref name="Yoshimoto"> PMID: 32447571</ref>. | The '''SARS-CoV-2 non-structural protein nsp3''' contains 1945 amino acids and is therefore the largest of the viruses proteins<ref name="Yoshimoto"> PMID: 32447571</ref>. | ||
Like its SARS-CoV counterpart, the nsp3 consists of several domains. The nomenclature as well as the counting of the domains is not always consistent. These domains are described in more detail below in order of their position within the protein, from the N- to the C-terminus: | Like its SARS-CoV counterpart, the nsp3 consists of several domains. The nomenclature as well as the counting of the domains is not always consistent. These domains are described in more detail below in order of their position within the protein, from the N- to the C-terminus: | ||
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The CoV-Y domain is conserved within coronaviruses, but its specific function is unclear<ref name="Lei"/>. | The CoV-Y domain is conserved within coronaviruses, but its specific function is unclear<ref name="Lei"/>. | ||
[[Image:TableNsp3domains2.png|500px|left|thumb|The domains of SARS-CoV-2 nsp3.]] | |||
==Disease== | ==Disease== | ||
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__NOTOC__ | __NOTOC__ | ||
</SX> | </SX> | ||
== See also == | |||
[[Coronavirus_Disease 2019 (COVID-19)]]<br> | |||
[[SARS-CoV-2_virus_proteins]]<br> | |||
[[COVID-19 AlphaFold2 Models]] | |||
== References == | == References == | ||
<references/> | <references/> | ||