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Literature summary for 3.4.17.23 extracted from

  • Shahbazi, B.; Mafakher, L.; Teimoori-Toolabi, L.
    Different compounds against Angiotensin-Converting Enzyme 2 (ACE2) receptor potentially containing the infectivity of SARS-CoV-2 an in silico study (2022), J. Mol. Model., 28, 82 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the SARS-CoV-2 chimeric receptor binding domain with human ACE2 complex. Residues Ser19, Gln24, Thr27, Phe28, His34, Glu35, Asp38, Tyr41, Gln42, Leu45, Tyr83, Asn330, Lys353, Gly354, Asp355, and Arg357 have a critical role in the binding regions. SARS-CoV has relatively similar interaction binding sites to SARS-CoV-2 except for Ser19, Leu45, Leu79, Gln325, Gly326, and Glu329 which are not involved in the interaction in SARS-CoV-2 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
chrysin shows a strong affinity for the active site of ACE2, ACE2-inhibitor complexes display structural stability with suitable binding energies. The interaction of chrysin with Phe40, Asp350, and Gly352 on ACE2 can interfere with the binding of SARS-CoV-2 Homo sapiens
luteolin shows a strong affinity for the active site of ACE2, ACE2-inhibitor complexes display structural stability with suitable binding energies Homo sapiens
pimozide effectively binds to the ACE2 binding site for SARS-CoV-2 spike protein, does not show stability during molecular dynamics simulation Homo sapiens
Ursodeoxycholic acid effectively binds to the ACE2 binding site for SARS-CoV-2 spike protein, does not show stability during molecular dynamics simulation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BYF1
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