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10.1021/acs.jpclett.1c02788

http://scihub22266oqcxt.onion/10.1021/acs.jpclett.1c02788
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34766775!ä!34766775

suck abstract from ncbi


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pmid34766775      J+Phys+Chem+Lett 2021 ; 12 (46): 11267-11272
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  • Interaction Analysis on the SARS-CoV-2 Spike Protein Receptor Binding Domain Using Visualization of the Interfacial Electrostatic Complementarity #MMPMID34766775
  • Ishikawa T; Ozono H; Akisawa K; Hatada R; Okuwaki K; Mochizuki Y
  • J Phys Chem Lett 2021[Nov]; 12 (46): 11267-11272 PMID34766775show ga
  • Visualization of the interfacial electrostatic complementarity (VIINEC) is a recently developed method for analyzing protein-protein interactions using electrostatic potential (ESP) calculated via the ab initio fragment molecular orbital method. In this Letter, the molecular interactions of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein with human angiotensin-converting enzyme 2 (ACE2) and B38 neutralizing antibody were examined as an illustrative application of VIINEC. The results of VIINEC revealed that the E484 of RBD has a role in making a local electrostatic complementary with ACE2 at the protein-protein interface, while it causes a considerable repulsive electrostatic interaction. Furthermore, the calculated ESP map at the interface of the RBD/B38 complex was significantly different from that of the RBD/ACE2 complex, which is discussed herein in association with the mechanism of the specificity of the antibody binding to the target protein.
  • |*Spike Glycoprotein, Coronavirus[MESH]


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