nsp15 forms a hexamer

Stable Identifier
R-HSA-9694436
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
cytosol
ReviewStatus
5/5
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nsp15 forms a hexamer
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nsp15 of SARS-CoV-2 shares 88% sequence identity and 95% sequence similarity with nsp15 of SARS-CoV-1. Similar to its SARS-CoV-1 orthologue, nsp15 of SARS-CoV-2 forms a hexamerthat consists of a dimer of trimers. Hexamer formation is necessary for the endonuclease activity of nsp15. nsp15 preferentially cleaves 3' of uridines, generating 2'-3' cyclic phosphates after cleavage. nsp15 requires Mn2+ ions for catalytic activity. C-terminal domain contains the active site, which faces away from the center of the hexamer and contains the extreme C-terminal residues (Kim et al. 2020).
Literature References
PubMed ID Title Journal Year
32803198 Cryo-EM Structures of the SARS-CoV-2 Endoribonuclease Nsp15

Borgnia, MJ, Sobhany, M, Frazier, MN, Williams, JG, Hsu, AL, Gordon, J, Dandey, VP, Dillard, LB, Kocaman, S, Hayne, CK, Stewart, ZD, Stanley, RE, Deterding, LJ, Pillon, MC, Perera, L, Krahn, JM

bioRxiv 2020
32304108 Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2

Maltseva, NI, Joachimiak, A, Godzik, A, Jedrzejczak, R, Kim, Y, Endres, M, Wilamowski, M, Michalska, K

Protein Sci. 2020
Participants
Input
Output
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as an event of
Disease
Name Identifier Synonyms
COVID-19 DOID:0080600 2019 Novel Coronavirus (2019-nCoV), Wuhan seafood market pneumonia virus infection, 2019-nCoV infection, Wuhan coronavirus infection
Authored
Orlic-Milacic, M  (2020-08-12)
Senff-Ribeiro, A  (2020-08-12)
Reviewed
Acencio, ML  (2020-09-09)
Created
Cook, J  (2020-07-07)
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