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10.1016/j.virusres.2021.198522

http://scihub22266oqcxt.onion/10.1016/j.virusres.2021.198522
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34314772!8310422!34314772
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suck abstract from ncbi


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pmid34314772      Virus+Res 2021 ; 303 (ä): 198522
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  • Structural modelling of SARS-CoV-2 alpha variant (B 1 1 7) suggests enhanced furin binding and infectivity #MMPMID34314772
  • Mohammad A; Abubaker J; Al-Mulla F
  • Virus Res 2021[Oct]; 303 (ä): 198522 PMID34314772show ga
  • The B.1.1.7 SARS-CoV-2 strain that has emerged in the UK in early December presents seven mutations and three deletions on S-protein structure that could lead to a more infective strain. The P681H mutation in the "PRRAR" furin cleavage site might affect the binding affinity to furin enzyme and hence its infectivity. Therefore, in this study, various structural bioinformatics approaches were used to model the S-protein structure with the B.1.1.7 variant amino acid substitutions and deletions. In addition to modelling the binding of furin to the cleavage site of the wild-type and the B.1.1.7 variant. Conclusively the B.1.1.7 variant resulted in dynamic stability, conformational changes and variations in binding energies in the S-protein structure, resulting in a more favourable binding of furin enzyme to the SARS-CoV-2 S-protein.
  • |Binding Sites[MESH]
  • |Furin/chemistry/*metabolism[MESH]
  • |Models, Molecular[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Mutation[MESH]
  • |Protein Binding[MESH]
  • |Protein Conformation[MESH]
  • |SARS-CoV-2/chemistry/genetics/*physiology[MESH]


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