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Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4

sagepub. 2018-11; 
Andrew J. Staup1 , Ivon U. De Silva1 , Justin T. Catt1 , Xuan Tan1 , Robert G. Hammond1 , and Margaret A. Johnson2
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Codon Optimization The residues 1445 to 1522 of nsp3 were amplified from a codon-optimized synthetic gene (Genscript, Piscataway, NJ, USA)35 and cloned into the vector pET-15b-TE (Northeast Structural Genomics Consortium and DNASu) encoding a N-terminal 6xHis tag. Get A Quote

摘要

Coronaviruses (CoVs) that cause infections such as severe acute respiratory syndrome (SARS) and Middle East respiratorysyndrome phylogenetically originate from bat CoVs. The coronaviral nonstructural protein 3 (nsp3) has been implicated inviral replication, polyprotein cleavage, and host immune interference. We report the structure of the C domain from theSARS-Unique Domain of bat CoV HKU4. The protein has a frataxin fold, consisting of 5 antiparallel β strands packed against2 α helices. Bioinformatics analyses and nuclear magnetic resonance experiments were conducted to investigate the functionof HKU4 C. The results showed that HKU4 C engages in protein-protein interactions with the nearby M domain of nsp3.T... More

關鍵詞

SARS-unique domain, coronavirus, non-structural protein, NMR, chemical shift perturbation, MERS, functional annotation
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