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PDBsum entry 6pxh
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Immune system/viral protein
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PDB id
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6pxh
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Contents |
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334 a.a.
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213 a.a.
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218 a.a.
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PDB id:
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| Name: |
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Immune system/viral protein
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Title:
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Crystal structure of mers-cov s1-ntd bound with g2 fab
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Structure:
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Mers-cov s1-ntd. Chain: a, b. Engineered: yes. G2 heavy chain. Chain: c, h. Engineered: yes. G2 light chain. Chain: d, l. Engineered: yes
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Source:
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Middle east respiratory syndrome-related coronavirus. Organism_taxid: 1335626. Expressed in: homo sapiens. Expression_system_taxid: 9606. Mus musculus. Organism_taxid: 10090. Expression_system_taxid: 9606
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Resolution:
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2.30Å
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R-factor:
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0.181
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R-free:
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0.213
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Authors:
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N.Wang,J.S.Mclellan
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Key ref:
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N.Wang
et al.
(2019).
Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.
Cell Rep,
28,
3395.
PubMed id:
DOI:
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Date:
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26-Jul-19
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Release date:
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25-Sep-19
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PROCHECK
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Headers
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References
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K9N5Q8
(SPIKE_CVEMC) -
Spike glycoprotein from Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012)
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Seq:
Struc:
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1353 a.a.
334 a.a.
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DOI no:
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Cell Rep
28:3395
(2019)
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PubMed id:
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Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.
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N.Wang,
O.Rosen,
L.Wang,
H.L.Turner,
L.J.Stevens,
K.S.Corbett,
C.A.Bowman,
J.Pallesen,
W.Shi,
Y.Zhang,
K.Leung,
R.N.Kirchdoerfer,
M.M.Becker,
M.R.Denison,
J.D.Chappell,
A.B.Ward,
B.S.Graham,
J.S.McLellan.
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ABSTRACT
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Middle East respiratory syndrome coronavirus (MERS-CoV) emerged into the human
population in 2012 and has caused substantial morbidity and mortality. Potently
neutralizing antibodies targeting the receptor-binding domain (RBD) on MERS-CoV
spike (S) protein have been characterized, but much less is known about
antibodies targeting non-RBD epitopes. Here, we report the structural and
functional characterization of G2, a neutralizing antibody targeting the
MERS-CoV S1 N-terminal domain (S1-NTD). Structures of G2 alone and in complex
with the MERS-CoV S1-NTD define a site of vulnerability comprising two loops,
each of which contain a residue mutated in G2-escape variants. Cell-surface
binding studies and in vitro competition experiments demonstrate that G2
strongly disrupts the attachment of MERS-CoV S to its receptor, dipeptidyl
peptidase-4 (DPP4), with the inhibition requiring the native trimeric S
conformation. These results advance our understanding of antibody-mediated
neutralization of coronaviruses and should facilitate the development of
immunotherapeutics and vaccines against MERS-CoV.
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Links
