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Basic Characteristics of Mutations
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Mutation Site
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D614G |
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Mutation Site Sentence
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Structural impact on SARS-CoV-2 spike protein by D614G substitution. |
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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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S |
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Standardized Encoding Gene
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S
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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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COVID-19
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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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33727252
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Title
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Structural impact on SARS-CoV-2 spike protein by D614G substitution
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Author
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Zhang J,Cai Y,Xiao T,Lu J,Peng H,Sterling SM,Walsh RM Jr,Rits-Volloch S,Zhu H,Woosley AN,Yang W,Sliz P,Chen B
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Journal
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Science (New York, N.Y.)
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Journal Info
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2021 Apr 30;372(6541):525-530
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Abstract
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Substitution for aspartic acid (D) by glycine (G) at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. Here, we report cryo-electron microscopy structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations that differ primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer-effectively increasing the number of functional spikes and enhancing infectivity-and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development.
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Sequence Data
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-
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