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* Residue conservation analysis
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DOI no:
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Proc Natl Acad Sci U S A
103:13985-13990
(2006)
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PubMed id:
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Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta.
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L.Zhang,
M.Derider,
M.A.McCornack,
S.C.Jao,
N.Isern,
T.Ness,
R.Moyer,
P.J.LiWang.
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ABSTRACT
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Chemokines (chemotactic cytokines) comprise a large family of proteins that
recruit and activate leukocytes, giving chemokines a major role in both immune
response and inflammation-related diseases. The poxvirus-encoded viral CC
chemokine inhibitor (vCCI) binds to many CC chemokines with high affinity,
acting as a potent inhibitor of chemokine action. We have used heteronuclear
multidimensional NMR to determine the structure of an orthopoxvirus vCCI in
complex with a human CC chemokine, MIP-1beta (macrophage inflammatory protein
1beta). vCCI binds to the chemokine with 1:1 stoichiometry, forming a complex of
311 aa. vCCI uses residues from its beta-sheet II to interact with a surface of
MIP-1beta that includes residues adjacent to its N terminus, as well as residues
in the 20's region and the 40's loop. This structure reveals the strategy used
by vCCI to tightly bind numerous chemokines while retaining selectivity for the
CC chemokine subfamily.
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Selected figure(s)
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Figure 3.
Fig. 3. Solution structure of the vCCI:MIP-1  complex.
Superposition of 15 NMR structures is shown, with the vCCI
backbone colored red and selected side chains colored pink. The
MIP-1 backbone is blue, and
selected side chains are shown in green.
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Figure 4.
Fig. 4. Detailed views of the VCCI:MIP–1 interaction. (A) MIP-1
Phe-13 (green) and the
surrounding hydrophobic residues (yellow) from vCCI. (B) View of
the 20's region and the 40's loop of MIP-1 (green) in proximity to
vCCI acidic residues (red). In the present structure, MIP-1 residues
45, 46, and 48 are changed to Ala to enhance solubility.
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Figures were
selected
by the author.
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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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D.V.Antonets,
T.S.Nepomnyashchikh,
and
S.N.Shchelkunov
(2010).
SECRET domain of variola virus CrmB protein can be a member of poxviral type II chemokine-binding proteins family.
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BMC Res Notes,
3,
271.
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C.A.Bursill,
E.McNeill,
L.Wang,
O.C.Hibbitt,
R.Wade-Martins,
D.J.Paterson,
D.R.Greaves,
and
K.M.Channon
(2009).
Lentiviral gene transfer to reduce atherosclerosis progression by long-term CC-chemokine inhibition.
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Gene Ther,
16,
93.
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J.M.Dias,
C.Losberger,
M.Déruaz,
C.A.Power,
A.E.Proudfoot,
and
J.P.Shaw
(2009).
Structural basis of chemokine sequestration by a tick chemokine binding protein: the crystal structure of the complex between Evasin-1 and CCL3.
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PLoS One,
4,
e8514.
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PDB codes:
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K.Van Vliet,
M.R.Mohamed,
L.Zhang,
N.Y.Villa,
S.J.Werden,
J.Liu,
and
G.McFadden
(2009).
Poxvirus proteomics and virus-host protein interactions.
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Microbiol Mol Biol Rev,
73,
730-749.
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J.M.Jones,
I.Messauodi,
R.D.Estep,
B.Orzechowska,
and
S.W.Wong
(2008).
Monkeypox virus viral chemokine inhibitor (MPV vCCI), a potent inhibitor of rhesus macrophage inflammatory protein-1.
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Cytokine,
43,
220-228.
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L.Deng,
P.Dai,
T.Parikh,
H.Cao,
V.Bhoj,
Q.Sun,
Z.Chen,
T.Merghoub,
A.Houghton,
and
S.Shuman
(2008).
Vaccinia virus subverts a mitochondrial antiviral signaling protein-dependent innate immune response in keratinocytes through its double-stranded RNA binding protein, E3.
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J Virol,
82,
10735-10746.
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M.B.Ruiz-Argüello,
V.P.Smith,
G.S.Campanella,
F.Baleux,
F.Arenzana-Seisdedos,
A.D.Luster,
and
A.Alcami
(2008).
An ectromelia virus protein that interacts with chemokines through their glycosaminoglycan binding domain.
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J Virol,
82,
917-926.
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M.W.Bahar,
J.C.Kenyon,
M.M.Putz,
N.G.Abrescia,
J.E.Pease,
E.L.Wise,
D.I.Stuart,
G.L.Smith,
and
J.M.Grimes
(2008).
Structure and function of A41, a vaccinia virus chemokine binding protein.
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PLoS Pathog,
4,
e5.
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PDB code:
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J.M.Alexander-Brett,
and
D.H.Fremont
(2007).
Dual GPCR and GAG mimicry by the M3 chemokine decoy receptor.
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J Exp Med,
204,
3157-3172.
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PDB codes:
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P.Sun,
B.P.Austin,
F.D.Schubot,
and
D.S.Waugh
(2007).
New protein fold revealed by a 1.65 A resolution crystal structure of Francisella tularensis pathogenicity island protein IglC.
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Protein Sci,
16,
2560-2563.
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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
codes are
shown on the right.
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Links
