Literature summary for 3.4.17.23 extracted from

Mannar, D.; Saville, J.; Zhu, X.; Srivastava, S.; Berezuk, A.; Tuttle, K.; Marquez, A.; Sekirov, I.; Subramaniam, S.
SARS-CoV-2 Omicron variant Antibody evasion and cryo-EM structure of spike protein-ACE2 complex (2022), Science, 375, 760-764 .

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Application

Application	Comment	Organism
medicine	interaction of ACE2 and SARS-CoV-2 Omicron spike protein. The mutations in the Omicron variant at residues 493, 496, 498, and 501 restore ACE2 binding efficiency that would be lost as a result of other mutations such as K417N	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
cryo-electron microscopy structure of ACE2 in complex with the SARS-CoV-2 Omicron variant spike protein reveals new salt bridges and hydrogen bonds formed by mutated residues Arg493, Ser496, and Arg498 in the receptor binding domain of spike protein. These interactions compensate for other Omicron mutations known to reduce ACE2 binding affinity, resulting in similar biochemical ACE2 binding affinities for the Delta and Omicron variants. Pseudoviruses that display the Omicron spike protein exhibit increased antibody evasion	Homo sapiens

Crystallization (Comment)

Organism

cryo-electron microscopy structure of ACE2 in complex with the SARS-CoV-2 Omicron variant spike protein reveals new salt bridges and hydrogen bonds formed by mutated residues Arg493, Ser496, and Arg498 in the receptor binding domain of spike protein. These interactions compensate for other Omicron mutations known to reduce ACE2 binding affinity, resulting in similar biochemical ACE2 binding affinities for the Delta and Omicron variants. Pseudoviruses that display the Omicron spike protein exhibit increased antibody evasion

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BYF1	-	-

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Release 2023.1 (January 2023)