Literature summary for 3.4.17.23 extracted from

Samanta, A.; Alam, S.; Ali, S.; Hoque, M.
Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variant (2022), EXCLI J., 21, 610-620 .

No PubMed abstract available

Search for more literature for 3.4.17.23

Crystallization (Commentary)

Crystallization (Comment)	Organism
interaction of ACE2 and the receptor-binding domain of SARS-CoV-2 spike protein. The omicron variant interacts with the ACE2 receptor with strong affinity involving unique amino acid residues than most of the SARS-CoV-2 variants suggesting increased infectivity and immune/vaccine evasion potential of the variant. The Lamda variant (C.37) interacts with ACE2 with higher affinity using identical receptor-binding domain residues as the omicron	Homo sapiens

Crystallization (Comment)

Organism

interaction of ACE2 and the receptor-binding domain of SARS-CoV-2 spike protein. The omicron variant interacts with the ACE2 receptor with strong affinity involving unique amino acid residues than most of the SARS-CoV-2 variants suggesting increased infectivity and immune/vaccine evasion potential of the variant. The Lamda variant (C.37) interacts with ACE2 with higher affinity using identical receptor-binding domain residues as the omicron

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BYF1	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)