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10.1016/j.jinf.2020.02.026

http://scihub22266oqcxt.onion/10.1016/j.jinf.2020.02.026
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32169481!7102553!32169481
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suck abstract from ncbi


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pmid32169481      J+Infect 2020 ; 80 (5): 554-562
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  • COVID-19 spike-host cell receptor GRP78 binding site prediction #MMPMID32169481
  • Ibrahim IM; Abdelmalek DH; Elshahat ME; Elfiky AA
  • J Infect 2020[May]; 80 (5): 554-562 PMID32169481show ga
  • OBJECTIVES: Understanding the novel coronavirus (COVID-19) mode of host cell recognition may help to fight the disease and save lives. The spike protein of coronaviruses is the main driving force for host cell recognition. METHODS: In this study, the COVID-19 spike binding site to the cell-surface receptor (Glucose Regulated Protein 78 (GRP78)) is predicted using combined molecular modeling docking and structural bioinformatics. The COVID-19 spike protein is modeled using its counterpart, the SARS spike. RESULTS: Sequence and structural alignments show that four regions, in addition to its cyclic nature have sequence and physicochemical similarities to the cyclic Pep42. Protein-protein docking was performed to test the four regions of the spike that fit tightly in the GRP78 Substrate Binding Domain beta (SBDbeta). The docking pose revealed the involvement of the SBDbeta of GRP78 and the receptor-binding domain of the coronavirus spike protein in recognition of the host cell receptor. CONCLUSIONS: We reveal that the binding is more favorable between regions III (C391-C525) and IV (C480-C488) of the spike protein model and GRP78. Region IV is the main driving force for GRP78 binding with the predicted binding affinity of -9.8?kcal/mol. These nine residues can be used to develop therapeutics specific against COVID-19.
  • |*Models, Molecular[MESH]
  • |Betacoronavirus/*chemistry/metabolism[MESH]
  • |Binding Sites[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/metabolism/*virology[MESH]
  • |Endoplasmic Reticulum Chaperone BiP[MESH]
  • |Heat-Shock Proteins/*chemistry/metabolism[MESH]
  • |Humans[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/metabolism/*virology[MESH]
  • |Protein Domains[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |SARS-CoV-2[MESH]


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