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Details on Person The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein
| Class:Id | LiteratureReference:9683401 |
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| _displayName | The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein |
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| _timestamp | 2020-04-14 21:44:40 |
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| author | [Person:9681654] Imbert, Isabelle
[Person:9681601] Snijder, Eric J
[Person:9683396] Dimitrova, Maria
[Person:9681647] Guillemot, Jean-Claude
[Person:9683402] Lécine, Patrick
[Person:9681646] Canard, Bruno |
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| created | [InstanceEdit:9683395] Orlic-Milacic, Marija, 2020-04-14 |
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| journal | Virus Res. |
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| pages | 136-48 |
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| pubMedIdentifier | 18255185 |
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| title | The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein |
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| volume | 133 |
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| year | 2008 |
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| (literatureReference) | [Reaction:9683393] nsp15 binds nsp8 [Homo sapiens]
[BlackBoxEvent:9686005] nsp3 binds to nsp7-8 and nsp12-16 [Homo sapiens]
[Summation:9683399] Nonstructural protein 15 (nsp15) of the SARS coronavirus (SA...
[Summation:9694519] This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.
On the final assembly, proteomics data suggest that the NAB−βSM−TM1 domains of nsp3 can interact with nsp7 − 8, as well as nsps 12–16, and the domain Y1 plus CoV-Y interacts with nsp9 and nsp12 (Imbert et al., 2008). Also a PL2pro−NAB−βSM−TM1 construct of Nsp3 can bind Nsp4 and Nsp12, while the region from TM1 to the end of Nsp3 only binds Nsp8 (Pan et al., 2008).
[Summation:9694624] This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.
Nonstructural protein 15 (nsp15) of the SARS coronavirus (SARS-CoV-1) binds to the replication-transcription complex (RTC) through interaction with nsp8 (Imbert et al. 2008). This interaction appears to be conserved in other coronaviruses, such as mouse hepatitis virus (MHV) (Athmer et al. 2017). nsp15 is an endonuclease characteristic for the order Nidovirales that includes the family Coronaviridae. nsp15 preferentially cleaves 3' of uridines, generating 2'-3' cyclic phosphates after cleavage. nsp15 requires Mn2+ ions for catalytic activity. Functional nsp15 is needed for production of viable virions and for viral transcription (Guarino et al. 2005, Ricagno et al. 2006, Bhardwaj et al. 2006, Joseph et al. 2007, Bhardwaj et al. 2008, Bhardwaj et al. 2012). The biological role of nsp15 has not been elucidated. It may degrade host mRNAs to shut down host translation, but so far no human or viral RNA targets have been identified.
[Summation:9711011] Severe acute respiratory syndrome coronavirus type 1 (SARS-C... |
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