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Details on Person Nonstructural protein 15 (nsp15) of the SARS coronavirus (SA...

Class:IdSummation:9683399
_displayNameNonstructural protein 15 (nsp15) of the SARS coronavirus (SA...
_timestamp2021-10-07 04:44:57
created[InstanceEdit:9683395] Orlic-Milacic, Marija, 2020-04-14
literatureReference[LiteratureReference:9683401] The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein
[LiteratureReference:9683400] In Situ Tagged nsp15 Reveals Interactions with Coronavirus Replication/Transcription Complex-Associated Proteins
[LiteratureReference:9682714] The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein
[LiteratureReference:9683204] Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15
[LiteratureReference:9683208] Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch
[LiteratureReference:9683220] Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family
[LiteratureReference:9683386] RNA recognition and cleavage by the SARS coronavirus endoribonuclease
[LiteratureReference:9683389] Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation
modified[InstanceEdit:9683407] Orlic-Milacic, Marija, 2020-04-15
[InstanceEdit:9755234] Shamovsky, Veronica, 2021-10-07
textNonstructural 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)[Reaction:9683393] nsp15 binds nsp8 [Homo sapiens]
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