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PDBsum entry 7nx7
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Viral protein/immune system
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PDB id
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7nx7
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Contents |
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214 a.a.
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214 a.a.
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193 a.a.
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214 a.a.
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213 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 k417n mutant receptor binding domain of sars- cov-2 spike glycoprotein in complex with covox-222 and ey6a fabs
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Structure:
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Ey6a fab heavy chain. Chain: h. Engineered: yes. Ey6a fab light chain. Chain: l. Engineered: yes. Spike protein s1. Chain: e. Engineered: yes.
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Source:
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Homo sapiens. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Severe acute respiratory syndrome coronavirus 2. 2019-ncov, sars-cov-2. Organism_taxid: 2697049. Gene: s, 2.
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Resolution:
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2.30Å
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R-factor:
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0.209
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R-free:
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0.239
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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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W.Dejnirattisai
et al.
(2021).
Antibody evasion by the P.1 strain of SARS-CoV-2.
Cell,
184,
2939.
PubMed id:
DOI:
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Date:
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17-Mar-21
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Release date:
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07-Apr-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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No UniProt id for this chain
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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.
193 a.a.*
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DOI no:
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Cell
184:2939
(2021)
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PubMed id:
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Antibody evasion by the P.1 strain of SARS-CoV-2.
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W.Dejnirattisai,
D.Zhou,
P.Supasa,
C.Liu,
A.J.Mentzer,
H.M.Ginn,
Y.Zhao,
H.M.E.Duyvesteyn,
A.Tuekprakhon,
R.Nutalai,
B.Wang,
C.López-Camacho,
J.Slon-Campos,
T.S.Walter,
D.Skelly,
S.A.Costa Clemens,
F.G.Naveca,
V.Nascimento,
F.Nascimento,
C.Fernandes da Costa,
P.C.Resende,
A.Pauvolid-Correa,
M.M.Siqueira,
C.Dold,
R.Levin,
T.Dong,
A.J.Pollard,
J.C.Knight,
D.Crook,
T.Lambe,
E.Clutterbuck,
S.Bibi,
A.Flaxman,
M.Bittaye,
S.Belij-Rammerstorfer,
S.C.Gilbert,
M.W.Carroll,
P.Klenerman,
E.Barnes,
S.J.Dunachie,
N.G.Paterson,
M.A.Williams,
D.R.Hall,
R.J.G.Hulswit,
T.A.Bowden,
E.E.Fry,
J.Mongkolsapaya,
J.Ren,
D.I.Stuart,
G.R.Screaton.
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ABSTRACT
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Terminating the SARS-CoV-2 pandemic relies upon pan-global vaccination. Current
vaccines elicit neutralizing antibody responses to the virus spike derived from
early isolates. However, new strains have emerged with multiple mutations,
including P.1 from Brazil, B.1.351 from South Africa, and B.1.1.7 from the UK
(12, 10, and 9 changes in the spike, respectively). All have mutations in the
ACE2 binding site, with P.1 and B.1.351 having a virtually identical triplet
(E484K, K417N/T, and N501Y), which we show confer similar increased affinity for
ACE2. We show that, surprisingly, P.1 is significantly less resistant to
naturally acquired or vaccine-induced antibody responses than B.1.351,
suggesting that changes outside the receptor-binding domain (RBD) impact
neutralization. Monoclonal antibody (mAb) 222 neutralizes all three variants
despite interacting with two of the ACE2-binding site mutations. We explain this
through structural analysis and use the 222 light chain to largely restore
neutralization potency to a major class of public antibodies.
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