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PDBsum entry 7d0b
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Viral protein/immune system
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PDB id
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7d0b
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Contents |
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1006 a.a.
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125 a.a.
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113 a.a.
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PDB id:
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| Name: |
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Viral protein/immune system
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Title:
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S protein of sars-cov-2 in complex bound with p5a-3c12_1b
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Structure:
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Spike glycoprotein. Chain: a, b, c. Synonym: s glycoprotein,e2,peplomer protein. Engineered: yes. Mutation: yes. Heavy chain of p5a-3c12. Chain: h. Engineered: yes. Light chain of p5a-3c12.
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Source:
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Severe acute respiratory syndrome coronavirus 2. 2019-ncov. Organism_taxid: 2697049. Gene: s, 2. Expressed in: homo sapiens. Expression_system_taxid: 9606. Homo sapiens. Human.
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Authors:
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R.H.Yan,R.K.Wang,B.Ju,J.F.Yu,Y.Y.Zhang,N.Liu,H.W.Wang,X.Q.Wang, L.Q.Zhang,Q.Zhou
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Key ref:
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R.Yan
et al.
(2021).
Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies.
Cell Res,
31,
517-525.
PubMed id:
DOI:
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Date:
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09-Sep-20
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Release date:
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10-Mar-21
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PROCHECK
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Headers
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References
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P0DTC2
(SPIKE_SARS2) -
Spike glycoprotein from Severe acute respiratory syndrome coronavirus 2
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Seq:
Struc:
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1273 a.a.
1006 a.a.*
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DOI no:
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Cell Res
31:517-525
(2021)
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PubMed id:
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Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies.
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R.Yan,
R.Wang,
B.Ju,
J.Yu,
Y.Zhang,
N.Liu,
J.Wang,
Q.Zhang,
P.Chen,
B.Zhou,
Y.Li,
Y.Shen,
S.Zhang,
L.Tian,
Y.Guo,
L.Xia,
X.Zhong,
L.Cheng,
X.Ge,
J.Zhao,
H.W.Wang,
X.Wang,
Z.Zhang,
L.Zhang,
Q.Zhou.
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ABSTRACT
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Neutralizing monoclonal antibodies (nAbs) to severe acute respiratory syndrome
coronavirus 2 (SARS-CoV-2) represent promising candidates for clinical
intervention against coronavirus disease 2019 (COVID-19). 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). However, the
structural basis for their potent neutralizing activity remains unclear. 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. The bivalent binding of the full-length IgG is found to
associate with more RBDs in the "up" conformation than the monovalent
binding of Fab, perhaps contributing to the enhanced neutralizing activity of
IgG and triggering more shedding of the S1 subunit from the S protein.
Comparison of a large number of nAbs identified common and unique structural
features associated with their potent neutralizing activities. This work
provides a structural basis for further understanding the mechanism of nAbs,
especially through revealing the bivalent binding and its correlation with more
potent neutralization and the shedding of S1 subunit.
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Links
