Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.17.23 extracted from

  • Han, P.; Li, L.; Liu, S.; Wang, Q.; Zhang, D.; Xu, Z.; Han, P.; Li, X.; Peng, Q.; Su, C.; Huang, B.; Li, D.; Zhang, R.; Tian, M.; Fu, L.; Gao, Y.; Zhao, X.; Liu, K.; Qi, J.; Gao, G.F.; Wang, P.
    Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 (2022), Cell, 185, 630-640.e10 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.17.23

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Homo sapiens Q9BYF1
-
-

General Information

General Information Comment Organism
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