Title : Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies.

Pub. Date : 2021 May

PMID : 33731853






3 Functional Relationships(s)
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1 We isolated a large number of nAbs from SARS-CoV-2-infected individuals capable of disrupting proper interaction between the receptor binding domain (RBD) of the viral spike (S) protein and the receptor angiotensin converting enzyme 2 (ACE2). nabs surface glycoprotein Severe acute respiratory syndrome coronavirus 2
2 We isolated a large number of nAbs from SARS-CoV-2-infected individuals capable of disrupting proper interaction between the receptor binding domain (RBD) of the viral spike (S) protein and the receptor angiotensin converting enzyme 2 (ACE2). nabs surface glycoprotein Severe acute respiratory syndrome coronavirus 2
3 Here, we report cryo-EM structures of the ten most potent nAbs in their native full-length IgG-form or in both IgG-form and Fab-form bound to the trimeric S protein of SARS-CoV-2. nabs surface glycoprotein Severe acute respiratory syndrome coronavirus 2