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PDBsum entry 6f9c
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(+ 0 more)
301 a.a.
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(+ 0 more)
431 a.a.
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PDB id:
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Virus
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Title:
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Model of the rift valley fever virus glycoprotein hexamer type 1
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Structure:
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Glycoprotein. Chain: a, c, e, g, i, k. Engineered: yes. Glycoprotein. Chain: b, d, f, h, j, l. Engineered: yes
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Source:
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Rift valley fever virus. Rvfv. Organism_taxid: 11588. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_taxid: 9606
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Authors:
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S.Halldorsson,T.A.Bowden,J.T.Huiskonen
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Key ref:
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S.Halldorsson
et al.
(2018).
Shielding and activation of a viral membrane fusion protein.
Nat Commun,
9,
349.
PubMed id:
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Date:
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14-Dec-17
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Release date:
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31-Jan-18
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PROCHECK
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Headers
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References
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Nat Commun
9:349
(2018)
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PubMed id:
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Shielding and activation of a viral membrane fusion protein.
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S.Halldorsson,
S.Li,
M.Li,
K.Harlos,
T.A.Bowden,
J.T.Huiskonen.
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ABSTRACT
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Entry of enveloped viruses relies on insertion of hydrophobic residues of the
viral fusion protein into the host cell membrane. However, the intermediate
conformations during fusion remain unknown. Here, we address the fusion
mechanism of Rift Valley fever virus. We determine the crystal structure of
the Gn glycoprotein and fit it with the Gc fusion protein into cryo-electron
microscopy reconstructions of the virion. Our analysis reveals how the Gn
shields the hydrophobic fusion loops of the Gc, preventing premature fusion.
Electron cryotomography of virions interacting with membranes under acidic
conditions reveals how the fusogenic Gc is activated upon removal of the Gn
shield. Repositioning of the Gn allows extension of Gc and insertion of fusion
loops in the outer leaflet of the target membrane. These data show early
structural transitions that enveloped viruses undergo during host cell entry and
indicate that analogous shielding mechanisms are utilized across diverse virus
families.
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');
}
}
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