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PDBsum entry 7neh
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Viral protein/immune system
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PDB id
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7neh
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Contents |
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219 a.a.
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215 a.a.
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196 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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Crystal structure of the receptor binding domain of sars-cov-2 spike glycoprotein in complex with covox-269 fab
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Structure:
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Covox-269 fab heavy chain. Chain: h. Engineered: yes. Covox-269 fab light chain. Chain: l. Engineered: yes. Spike glycoprotein. Chain: e. Synonym: s glycoprotein,e2,peplomer protein.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Severe acute respiratory syndrome coronavirus 2. 2019-ncov. Organism_taxid: 2697049.
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Resolution:
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1.77Å
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R-factor:
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0.189
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R-free:
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0.198
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Authors:
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D.Zhou,J.Ren,D.Stuart
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Key ref:
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P.Supasa
et al.
(2021).
Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.
Cell,
184,
2201.
PubMed id:
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Date:
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04-Feb-21
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Release date:
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03-Mar-21
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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Cell
184:2201
(2021)
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PubMed id:
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Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.
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P.Supasa,
D.Zhou,
W.Dejnirattisai,
C.Liu,
A.J.Mentzer,
H.M.Ginn,
Y.Zhao,
H.M.E.Duyvesteyn,
R.Nutalai,
A.Tuekprakhon,
B.Wang,
G.C.Paesen,
J.Slon-Campos,
C.López-Camacho,
B.Hallis,
N.Coombes,
K.R.Bewley,
S.Charlton,
T.S.Walter,
E.Barnes,
S.J.Dunachie,
D.Skelly,
S.F.Lumley,
N.Baker,
I.Shaik,
H.E.Humphries,
K.Godwin,
N.Gent,
A.Sienkiewicz,
C.Dold,
R.Levin,
T.Dong,
A.J.Pollard,
J.C.Knight,
P.Klenerman,
D.Crook,
T.Lambe,
E.Clutterbuck,
S.Bibi,
A.Flaxman,
M.Bittaye,
S.Belij-Rammerstorfer,
S.Gilbert,
D.R.Hall,
M.A.Williams,
N.G.Paterson,
W.James,
M.W.Carroll,
E.E.Fry,
J.Mongkolsapaya,
J.Ren,
D.I.Stuart,
G.R.Screaton.
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ABSTRACT
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SARS-CoV-2 has caused over 2 million deaths in little over a year. Vaccines are
being deployed at scale, aiming to generate responses against the virus spike.
The scale of the pandemic and error-prone virus replication is leading to the
appearance of mutant viruses and potentially escape from antibody responses.
Variant B.1.1.7, now dominant in the UK, with increased transmission, harbors 9
amino acid changes in the spike, including N501Y in the ACE2 interacting
surface. We examine the ability of B.1.1.7 to evade antibody responses elicited
by natural SARS-CoV-2 infection or vaccination. We map the impact of N501Y by
structure/function analysis of a large panel of well-characterized monoclonal
antibodies. B.1.1.7 is harder to neutralize than parental virus, compromising
neutralization by some members of a major class of public antibodies through
light-chain contacts with residue 501. However, widespread escape from
monoclonal antibodies or antibody responses generated by natural infection or
vaccination was not observed.
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Links
