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10.1039/d0cp03145c

http://scihub22266oqcxt.onion/10.1039/d0cp03145c
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32756685!ä!32756685

suck abstract from ncbi


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pmid32756685      Phys+Chem+Chem+Phys 2020 ; 22 (33): 18272-18283
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  • Intra- and intermolecular atomic-scale interactions in the receptor binding domain of SARS-CoV-2 spike protein: implication for ACE2 receptor binding #MMPMID32756685
  • Adhikari P; Li N; Shin M; Steinmetz NF; Twarock R; Podgornik R; Ching WY
  • Phys Chem Chem Phys 2020[Sep]; 22 (33): 18272-18283 PMID32756685show ga
  • The COVID-19 pandemic poses a severe threat to human health with unprecedented social and economic disruption. Spike (S) glycoprotein in the SARS-CoV-2 virus is pivotal in understanding the virus anatomy, since it initiates the early contact with the ACE2 receptor in the human cell. The subunit S1 in chain A of S-protein has four structural domains: the receptor binding domain (RBD), the n-terminal domain (NTD) and two subdomains (SD1, SD2). We report details of the intra- and inter-molecular binding mechanism of RBD using density functional theory, including electronic structure, interatomic bonding and partial charge distribution. We identify five strong hydrogen bonds and analyze their roles in binding. This provides a pathway to a quantum-chemical understanding of the interaction between the S-protein and the ACE2 receptor with insights into the function of conserved features in the ACE2 receptor binding domain that could inform vaccine and drug development.
  • |Amino Acid Sequence[MESH]
  • |Angiotensin-Converting Enzyme 2[MESH]
  • |Betacoronavirus/*chemistry[MESH]
  • |Density Functional Theory[MESH]
  • |Humans[MESH]
  • |Hydrogen Bonding[MESH]
  • |Models, Chemical[MESH]
  • |Peptidyl-Dipeptidase A/chemistry/*metabolism[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |SARS-CoV-2[MESH]
  • |Sequence Alignment[MESH]


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