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PDBsum entry 6zoz
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Viral protein
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PDB id
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6zoz
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PDB id:
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| Name: |
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Viral protein
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Title:
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Structure of disulphide-stabilized sars-cov-2 spike protein trimer (x1 disulphide-bond mutant, s383c, d985c, k986p, v987p, single arg s1/s2 cleavage site) in locked state
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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
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Source:
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Severe acute respiratory syndrome coronavirus 2. Organism_taxid: 2697049. Variant: s383c. Gene: s, 2. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: expi293
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Authors:
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X.Xiong,K.Qu,S.H.W.Scheres,J.A.G.Briggs
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Key ref:
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X.Xiong
et al.
(2020).
A thermostable, closed SARS-CoV-2 spike protein trimer.
Nat Struct Mol Biol,
27,
934-941.
PubMed id:
DOI:
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Date:
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08-Jul-20
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Release date:
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22-Jul-20
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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.
1069 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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DOI no:
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Nat Struct Mol Biol
27:934-941
(2020)
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PubMed id:
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A thermostable, closed SARS-CoV-2 spike protein trimer.
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X.Xiong,
K.Qu,
K.A.Ciazynska,
M.Hosmillo,
A.P.Carter,
S.Ebrahimi,
Z.Ke,
S.H.W.Scheres,
L.Bergamaschi,
G.L.Grice,
Y.Zhang,
J.A.Nathan,
S.Baker,
L.C.James,
H.E.Baxendale,
I.Goodfellow,
R.Doffinger,
J.A.G.Briggs,
J.Bradley,
P.A.Lyons,
K.G.C.Smith,
M.Toshner,
A.Elmer,
C.Ribeiro,
J.Kourampa,
S.Jose,
J.Kennet,
J.Rowlands,
A.Meadows,
C.O'Brien,
R.Rastall,
C.Crucusio,
S.Hewitt,
J.Price,
J.Calder,
L.Canna,
A.Bucke,
H.Tordesillas,
J.Harris,
V.Ruffolo,
J.Domingo,
B.Graves,
H.Butcher,
D.Caputo,
E.Le Gresley,
B.J.Dunmore,
J.Martin,
E.Legchenko,
C.Treacy,
C.Huang,
J.Wood,
R.Sutcliffe,
J.Hodgson,
J.Shih,
S.Graf,
Z.Tong,
F.Mescia,
T.Tilly,
C.O'Donnell,
K.Hunter,
L.Pointon,
N.Pond,
M.Wylot,
E.Jones,
S.Fawke,
B.Bullman,
L.Bergamaschi,
L.Turner,
I.Jarvis,
O.Omarjee,
A.De Sa,
J.Marsden,
A.Betancourt,
M.Perera,
M.Epping,
N.Richoz,
G.Bower,
R.Sharma,
F.Nice,
O.Huhn,
H.Stark,
N.Walker,
K.Stirrups,
N.Ovington,
E.Dewhust,
E.Li,
S.Papadia.
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ABSTRACT
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The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and
is the dominant target of the immune system. It exhibits substantial
conformational flexibility. It transitions from closed to open conformations to
expose its receptor-binding site and, subsequently, from prefusion to postfusion
conformations to mediate fusion of viral and cellular membranes. S-protein
derivatives are components of vaccine candidates and diagnostic assays, as well
as tools for research into the biology and immunology of SARS-CoV-2. Here we
have designed mutations in S that allow the production of thermostable,
disulfide-bonded S-protein trimers that are trapped in the closed, prefusion
state. Structures of the disulfide-stabilized and non-disulfide-stabilized
proteins reveal distinct closed and locked conformations of the S trimer. We
demonstrate that the designed, thermostable, closed S trimer can be used in
serological assays. This protein has potential applications as a reagent for
serology, virology and as an immunogen.
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