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PDBsum entry 1ea3
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Influenza virus
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PDB id
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1ea3
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Virology
279:439-446
(2001)
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PubMed id:
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Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer.
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S.Arzt,
F.Baudin,
A.Barge,
P.Timmins,
W.P.Burmeister,
R.W.Ruigrok.
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ABSTRACT
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The amino-terminal domain of influenza A virus matrix protein (residues 1-164)
was crystallized at pH 7 into a new crystal form in space group P1. This packing
of the protein implies that M1(1-164) was monomeric in solution when it
crystallized. Otherwise, the structure of the M1 fragment in the pH 7 crystals
was the same as the monomers in crystals formed at pH 4 where crystal packing
resulted in dimer formation [B. Sha and M. Luo, 1997, Nature Struct. Biol. 4,
239-244]. Analysis of intact M1 protein, the N-terminal domain, and the
remaining C-terminal fragment (residues 165-252) in solution also showed that
the N-terminal domain was monomeric with the same dimensions as determined from
the crystal structure. Intact M1 protein was also monomeric but with an
elongated shape due to the presence of the C-terminal part. Circular dichroism
showed that the C-terminal part of M1 contained helical structure. A model for
soluble M1 is presented, based on the assumption that the C-terminal domain is
spherical, in which the N- and C-terminal domains are connected by a linker
sequence which is available for proteolytic attack.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.J.Calder,
S.Wasilewski,
J.A.Berriman,
and
P.B.Rosenthal
(2010).
Structural organization of a filamentous influenza A virus.
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Proc Natl Acad Sci U S A,
107,
10685-10690.
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J.Zhang,
G.Li,
X.Liu,
Z.Wang,
W.Liu,
and
X.Ye
(2009).
Influenza A virus M1 blocks the classical complement pathway through interacting with C1qA.
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J Gen Virol,
90,
2751-2758.
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S.Huang,
J.Chen,
H.Wang,
B.Sun,
H.Wang,
Z.Zhang,
X.Zhang,
and
Z.Chen
(2009).
Influenza A virus matrix protein 1 interacts with hTFIIIC102-s, a short isoform of the polypeptide 3 subunit of human general transcription factor IIIC.
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Arch Virol,
154,
1101-1110.
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I.u.A.Smirnova,
L.V.Kordiukova,
M.V.Serebriakova,
I.I.u.Filippova,
E.N.Lysogorskaia,
and
L.A.Baratova
(2008).
[Flu virion as a substrate for proteolytic enzymes]
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Bioorg Khim,
34,
409-415.
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T.T.Lam,
C.C.Hon,
O.G.Pybus,
S.L.Kosakovsky Pond,
R.T.Wong,
C.W.Yip,
F.Zeng,
and
F.C.Leung
(2008).
Evolutionary and transmission dynamics of reassortant H5N1 influenza virus in Indonesia.
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PLoS Pathog,
4,
e1000130.
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S.L.Noton,
E.Medcalf,
D.Fisher,
A.E.Mullin,
D.Elton,
and
P.Digard
(2007).
Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions.
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J Gen Virol,
88,
2280-2290.
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E.K.Hui,
S.Barman,
D.H.Tang,
B.France,
and
D.P.Nayak
(2006).
YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42.
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J Virol,
80,
2291-2308.
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B.J.Chen,
M.Takeda,
and
R.A.Lamb
(2005).
Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.
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J Virol,
79,
13673-13684.
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D.Pasdeloup,
N.Poisson,
H.Raux,
Y.Gaudin,
R.W.Ruigrok,
and
D.Blondel
(2005).
Nucleocytoplasmic shuttling of the rabies virus P protein requires a nuclear localization signal and a CRM1-dependent nuclear export signal.
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Virology,
334,
284-293.
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E.Hoffmann,
K.Mahmood,
Z.Chen,
C.F.Yang,
J.Spaete,
H.B.Greenberg,
M.L.Herlocher,
H.Jin,
and
G.Kemble
(2005).
Multiple gene segments control the temperature sensitivity and attenuation phenotypes of ca B/Ann Arbor/1/66.
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J Virol,
79,
11014-11021.
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I.Garcia-Robles,
H.Akarsu,
C.W.Müller,
R.W.Ruigrok,
and
F.Baudin
(2005).
Interaction of influenza virus proteins with nucleosomes.
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Virology,
332,
329-336.
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L.M.Burleigh,
L.J.Calder,
J.J.Skehel,
and
D.A.Steinhauer
(2005).
Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.
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J Virol,
79,
1262-1270.
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M.F.McCown,
and
A.Pekosz
(2005).
The influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packaging.
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J Virol,
79,
3595-3605.
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J.Timmins,
R.W.Ruigrok,
and
W.Weissenhorn
(2004).
Structural studies on the Ebola virus matrix protein VP40 indicate that matrix proteins of enveloped RNA viruses are analogues but not homologues.
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FEMS Microbiol Lett,
233,
179-186.
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E.K.Hui,
S.Barman,
T.Y.Yang,
and
D.P.Nayak
(2003).
Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs.
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J Virol,
77,
7078-7092.
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H.Akarsu,
W.P.Burmeister,
C.Petosa,
I.Petit,
C.W.Müller,
R.W.Ruigrok,
and
F.Baudin
(2003).
Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2).
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EMBO J,
22,
4646-4655.
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PDB code:
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M.Gaudier,
Y.Gaudin,
and
M.Knossow
(2002).
Crystal structure of vesicular stomatitis virus matrix protein.
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EMBO J,
21,
2886-2892.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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