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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/1356| Structure of the SARS-unique domain C from the bat coronavirus HKU4 | |
| Staup, A De Silva, I Catt, J Tan, X Hammond, R Johnson, M | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| Coronaviruses (CoVs) that cause infections such as severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome phylogenetically originate from bat CoVs. The coronaviral nonstructural protein 3 (nsp3) has been implicated in viral replication, polyprotein cleavage, and host immune interference. We report the structure of the C domain from the SARS-Unique Domain of bat CoV HKU4. The protein has a frataxin fold, consisting of 5 antiparallel β strands packed against 2 α helices. Bioinformatics analyses and nuclear magnetic resonance experiments were conducted to investigate the function of HKU4 C. The results showed that HKU4 C engages in protein-protein interactions with the nearby M domain of nsp3. The HKU4 C residues involved in protein-protein interactions are conserved in group 2c CoVs, indicating a conserved function. | |
| Natural Product Communications | |
| 2019 | |
| Preimpreso | |
| https://coronavirus.1science.com/item/04ed3179d71cc1b8977500a498d00a1f8aae7208 | |
| Inglés | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Artículos científicos |
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| 108111.pdf | 2.18 MB | Adobe PDF | Visualizar/Abrir |