Crystallization (Comment) | Organism |
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structure of the complex with SARS-CoV-2 receptor-binding domains of variants omicron and delta. The substitutions in omicron receptor-binding domian lead to changes of electrostatic charges. Compared with other variant receptor-binding domains, the binding surface of omicron receptor-binding domain has the largest-scale positive charge region. T478K, Q493R, and Q498R substitutions significantly increase positive changes, and E484A decreases the negative charges | Homo sapiens |
Organism | UniProt | Comment | Textmining |
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Homo sapiens | Q9BYF1 | - |
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General Information | Comment | Organism |
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physiological function | ACE2 binds the prototype SARS-CoV-2 receptor-binding domain with a dissociation constant (KD) of 24.63 nM. Receptor-binding domains from SARS-CoV-2 variants alpha, beta, and gamma demonstrate enhanced affinities, ranging from 1.78- to 4.56fold increase. Variant omicron, along with delta receptor-binding domain, shows no significant change in binding affinities when compared with those of the prototype domain | Homo sapiens |