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PDBsum entry 5fvc
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Viral protein
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PDB id
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5fvc
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Contents |
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346 a.a.
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(+ 2 more)
367 a.a.
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References listed in PDB file
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Key reference
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Title
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Nucleocapsid assembly in pneumoviruses is regulated by conformational switching of the n protein.
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Authors
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M.Renner,
M.Bertinelli,
C.Leyrat,
G.C.Paesen,
L.F.Saraiva de oliveira,
J.T.Huiskonen,
J.M.Grimes.
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Ref.
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Elife, 2016,
5,
e12627.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Non-segmented, (-)RNA viruses cause serious human diseases. Human
metapneumovirus (HMPV), an emerging pathogen of this order of viruses
(Mononegavirales) is one of the main causes of respiratory tract illness in
children. To help elucidate the assembly mechanism of the nucleocapsid (the
viral RNA genome packaged by the nucleoprotein N) we present crystallographic
structures of HMPV N in its assembled RNA-bound state and in a monomeric state,
bound to the polymerase cofactor P. Our structures reveal molecular details of
how P inhibits the self-assembly of N and how N transitions between the RNA-free
and RNA-bound conformational state. Notably, we observe a role for the
C-terminal extension of N in directly preventing premature uptake of RNA by
folding into the RNA-binding cleft. Our structures suggest a common mechanism of
how the growth of the nucleocapsid is orchestrated, and highlight an interaction
site representing an important target for antivirals.
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