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PDBsum entry 2w2s
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Viral protein
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PDB id
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2w2s
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References listed in PDB file
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Key reference
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Title
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Rhabdovirus matrix protein structures reveal a novel mode of self-Association.
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Authors
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S.C.Graham,
R.Assenberg,
O.Delmas,
A.Verma,
A.Gholami,
C.Talbi,
R.J.Owens,
D.I.Stuart,
J.M.Grimes,
H.Bourhy.
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Ref.
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Plos Pathog, 2008,
4,
e1000251.
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PubMed id
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Abstract
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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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Secondary reference #1
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Title
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Expression, Purification and crystallization of a lyssavirus matrix (m) protein.
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Authors
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R.Assenberg,
O.Delmas,
S.C.Graham,
A.Verma,
N.Berrow,
D.I.Stuart,
R.J.Owens,
H.Bourhy,
J.M.Grimes.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
258-262.
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PubMed id
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