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Basic Characteristics of Mutations
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Mutation Site
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D48N |
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Mutation Site Sentence
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Structural Basis for the Inhibition of SARS-CoV-2 Mpro D48N Mutant by Shikonin and PF-07321332. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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Mpro |
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Standardized Encoding Gene
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ORF1a
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Genotype/Subtype
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- |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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-
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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38257765
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Title
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Structural Basis for the Inhibition of SARS-CoV-2 M(pro) D48N Mutant by Shikonin and PF-07321332
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Author
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Zhao Z,Zhu Q,Zhou X,Li W,Yin X,Li J
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Journal
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Viruses
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Journal Info
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2023 Dec 30;16(1):65
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Abstract
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Preventing the spread of SARS-CoV-2 and its variants is crucial in the fight against COVID-19. Inhibition of the main protease (M(pro)) of SARS-CoV-2 is the key to disrupting viral replication, making M(pro) a promising target for therapy. PF-07321332 and shikonin have been identified as effective broad-spectrum inhibitors of SARS-CoV-2 M(pro). The crystal structures of SARS-CoV-2 M(pro) bound to PF-07321332 and shikonin have been resolved in previous studies. However, the exact mechanism regarding how SARS-CoV-2 M(pro) mutants impact their binding modes largely remains to be investigated. In this study, we expressed a SARS-CoV-2 M(pro) mutant, carrying the D48N substitution, representing a class of mutations located near the active sites of M(pro). The crystal structures of M(pro) D48N in complex with PF-07321332 and shikonin were solved. A detailed analysis of the interactions between M(pro) D48N and two inhibitors provides key insights into the binding pattern and its structural determinants. Further, the binding patterns of the two inhibitors to M(pro) D48N mutant and wild-type M(pro) were compared in detail. This study illustrates the possible conformational changes when the M(pro) D48N mutant is bound to inhibitors. Structural insights derived from this study will inform the development of new drugs against novel coronaviruses.
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Sequence Data
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-
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