| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
Rhabdovirus matrix protein structures reveal a novel mode of self-association.
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| Autores: |
Graham, Stephen C.
Assenberg, René
Delmas, Olivier
Verma, Anil
Gholami, Alireza
Talbi, Chiraz
Owens, Raymond J.
Stuart, David I.
Grimes, Jonathan M.
Bourhy, Hervé
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| Data: |
2008
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| Ano: |
2008
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| Resumo: |
The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise-disordered N terminus of a crystallographically adjacent molecule is observed binding to a hydrophobic cavity on the surface of the protein, thereby forming non-covalent linear polymers of M in the crystals. While the overall topology of the interaction is conserved between the two structures, the molecular details of the interactions are completely different. The observed interactions provide a compelling model for the flexible self-assembly of the matrix protein during virion morphogenesis and may also modulate interactions with host proteins.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
http://archimer.ifremer.fr/doc/00139/24995/23093.pdf
DOI:10.1371/journal.ppat.1000251
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| Editor: |
Public Library Science
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| Relação: |
http://archimer.ifremer.fr/doc/00139/24995/
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| Formato: |
application/pdf
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| Fonte: |
PLOS pathogens (1553-7374) (Public Library Science), 2008 , Vol. 4 , N. 12 , P. 1-12
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| Direitos: |
2008 Graham et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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