Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
The SARS-CoV-2 main protease (Mpro) is one of two cysteine proteases essential for viral replication. Here, the authors determine the crystal structure of an Mpro acyl intermediate with its native C-terminal autocleavage sequence and the structure of a product bound active site mutant (C145A), which...
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| Autores principales: | , , , , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2020
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/79fa01c0d7f04a9ab66a27ea9f850fb5 |
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| Sumario: | The SARS-CoV-2 main protease (Mpro) is one of two cysteine proteases essential for viral replication. Here, the authors determine the crystal structure of an Mpro acyl intermediate with its native C-terminal autocleavage sequence and the structure of a product bound active site mutant (C145A), which are of interest for antiviral drug development. |
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