Literature summary for 3.4.17.23 extracted from

Cao, W.; Dong, C.; Kim, S.; Hou, D.; Tai, W.; Du, L.; Im, W.; Zhang, X.F.
Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction (2021), Biophys. J., 120, 1011-1019 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BYF1	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	SARSCoV-2 receptor-binding domain (RBD) interacts with the N-linked glycan on Asn90 of ACE2. This interaction is mostly absent in the SARS-CoV-1 RBDACE2 complex. After removing N-linked glycans on ACE2, its mechanical binding strength with SARS-CoV-2 RBD decreases to a similar level of the SARS-CoV-1 RBD-ACE2 interaction	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
HEK-293T cell	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
ACE2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (the virus causing COVID-19) is known to use the receptor-binding domain (RBD) at viral surface spike (S) protein to interact with the angiotensin-converting enzyme 2 (ACE2) receptor expressed on many human cell types. The RBD-ACE2 interaction is a crucial step to mediate the host cell entry of SARS-CoV-2.	Homo sapiens

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Release 2023.1 (January 2023)