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Literature summary for 3.4.17.23 extracted from
- Unbinding of hACE2 and inhibitors from the receptor binding domain of SARS-CoV-2 spike protein (2022), J. Biomol. Struct. Dyn., 2022, 1-20 .
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | inhibition of SARS-CoV-2 spike protein binding to ACE2 by a higher-affinity variant of the B38 monoclonal antibody, containing mutantion F27Q in the heavy chain (F27Q), which can bind to the rececptor-binding domain more tightly, and by Ty1 alpaca nanobody, i.e.a 38 amino acid peptide inhibitor taking components from Ty1. The peptide exhibits improved affinity for the rececptor-binding by up to 100fold, and like B38 mutant, it can outclass the binding affinity of ACE2 with the rececptor-binding domain | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the SARS-CoV-2 S/receptor-binding domain binding interface with ACE2 contains in total 17 residues of receptor-binding domain and 16 residues of ACE2 as interfacial residues in the protein-protein complex, forming H-bond, one salt bridge, and several van der Waals interactions. The receptor-binding domain of the spike protein has the highest affinity towards ACE2 in comparison to its two inhibitors B38 monoclonal antibody followed by Ty1 alpaca nanobody | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q9BYF1 | - |
- |
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