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PDBsum entry 6y9m
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Viral protein
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PDB id
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6y9m
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DOI no:
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Proc Natl Acad Sci U S A
117:26237-26244
(2020)
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PubMed id:
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Crystal structure of tomato spotted wilt virus GN reveals a dimer complex formation and evolutionary link to animal-infecting viruses.
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Y.Bahat,
J.Alter,
M.Dessau.
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ABSTRACT
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Tospoviridae is a family of enveloped RNA plant viruses that infect many
field crops, inflicting a heavy global economic burden. These tripartite,
single-stranded, negative-sense RNA viruses are transmitted from plant to plant
by thrips as the insect vector. The medium (M) segment of the viral genome
encodes two envelope glycoproteins, GN and GC, which
together form the envelope spikes. GC is considered the virus
fusogen, while the accompanying GN protein serves as an attachment
protein that binds to a yet unknown receptor, mediating the virus acquisition by
the thrips carrier. Here we present the crystal structure of glycoprotein N
(GN) from the tomato spotted wilt virus (TSWV), a representative
member of the Tospoviridae family. The structure suggests that
GN is organized as dimers on TSWV's outer shell. Our structural data
also suggest that this dimerization is required for maintaining GN
structural integrity. Although the structure of the TSWV GN is
different from other bunyavirus GN proteins, they all share similar
domain connectivity that resembles glycoproteins from unrelated animal-infecting
viruses, suggesting a common ancestor for these accompanying proteins.
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');
}
}
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