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PDBsum entry 1ncv
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* Residue conservation analysis
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DOI no:
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Biochemistry
36:4412-4422
(1997)
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PubMed id:
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Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy.
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S.Meunier,
J.M.Bernassau,
J.C.Guillemot,
P.Ferrara,
H.Darbon.
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ABSTRACT
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MCP-3 is a beta chemokine consisting of 76 amino acid residues. It has been
described to be involved in the activation of all leukocytic cells, activation
mediated by the presence of multiple binding sites on the target cells. Its
three-dimensional structure has been studied by making use of two-dimensional 1H
NMR spectroscopy. MCP-3 exhibits the same monomeric structure as the other
chemokines, i.e., a three-stranded antiparallel beta sheet covered on one face
by an alpha helix. Although it belongs to the same subfamily as RANTES (Chung et
al., 1995; Faitbrother et al., 1994) and hMIP-1beta (Lodi et al., 1994), the
MCP-3 dimer is folded like IL-8 with the so-called alphabeta sandwich structural
motif. Structural and sequence analysis gives clear indications suggesting that
the other MCP chemokines may have the same quaternary structure, contrary to the
other beta chemokines.
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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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S.L.Deshmane,
S.Kremlev,
S.Amini,
and
B.E.Sawaya
(2009).
Monocyte chemoattractant protein-1 (MCP-1): an overview.
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J Interferon Cytokine Res,
29,
313-326.
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C.Barinka,
A.Prahl,
and
J.Lubkowski
(2008).
Structure of human monocyte chemoattractant protein 4 (MCP-4/CCL13).
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Acta Crystallogr D Biol Crystallogr,
64,
273-278.
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PDB code:
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H.Jin,
X.Shen,
B.R.Baggett,
X.Kong,
and
P.J.LiWang
(2007).
The human CC chemokine MIP-1beta dimer is not competent to bind to the CCR5 receptor.
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J Biol Chem,
282,
27976-27983.
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D.M.Hoover,
C.Boulegue,
D.Yang,
J.J.Oppenheim,
K.Tucker,
W.Lu,
and
J.Lubkowski
(2002).
The structure of human macrophage inflammatory protein-3alpha /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human beta-defensins.
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J Biol Chem,
277,
37647-37654.
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PDB code:
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E.S.Kuloğlu,
D.R.McCaslin,
J.L.Markley,
and
B.F.Volkman
(2002).
Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions.
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J Biol Chem,
277,
17863-17870.
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H.Lortat-Jacob,
A.Grosdidier,
and
A.Imberty
(2002).
Structural diversity of heparan sulfate binding domains in chemokines.
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Proc Natl Acad Sci U S A,
99,
1229-1234.
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Buyong,
J.Xiong,
J.Lubkowski,
and
R.Nussinov
(2000).
Homology modeling and molecular dynamics simulations of lymphotactin.
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Protein Sci,
9,
2192-2199.
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J.Blaszczyk,
E.V.Coillie,
P.Proost,
J.V.Damme,
G.Opdenakker,
G.D.Bujacz,
J.M.Wang,
and
X.Ji
(2000).
Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors.
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Biochemistry,
39,
14075-14081.
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PDB code:
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J.S.Laurence,
C.Blanpain,
J.W.Burgner,
M.Parmentier,
and
P.J.LiWang
(2000).
CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding.
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Biochemistry,
39,
3401-3409.
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J.T.Ashfield,
T.Meyers,
D.Lowne,
P.G.Varley,
J.R.Arnold,
P.Tan,
J.C.Yang,
L.G.Czaplewski,
T.Dudgeon,
and
J.Fisher
(2000).
Chemical modification of a variant of human MIP-1alpha; implications for dimer structure.
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Protein Sci,
9,
2047-2053.
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K.L.Mayer,
and
M.J.Stone
(2000).
NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2.
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Biochemistry,
39,
8382-8395.
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PDB codes:
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A.C.LiWang,
J.J.Cao,
H.Zheng,
Z.Lu,
S.C.Peiper,
and
P.J.LiWang
(1999).
Dynamics study on the anti-human immunodeficiency virus chemokine viral macrophage-inflammatory protein-II (VMIP-II) reveals a fully monomeric protein.
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Biochemistry,
38,
442-453.
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A.C.Liwang,
Z.X.Wang,
Y.Sun,
S.C.Peiper,
and
P.J.Liwang
(1999).
The solution structure of the anti-HIV chemokine vMIP-II.
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Protein Sci,
8,
2270-2280.
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PDB code:
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E.Van Coillie,
J.Van Damme,
and
G.Opdenakker
(1999).
The MCP/eotaxin subfamily of CC chemokines.
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Cytokine Growth Factor Rev,
10,
61-86.
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H.Sticht,
S.E.Escher,
K.Schweimer,
W.G.Forssmann,
P.Rösch,
and
K.Adermann
(1999).
Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
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Biochemistry,
38,
5995-6002.
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PDB code:
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L.G.Czaplewski,
J.McKeating,
C.J.Craven,
L.D.Higgins,
V.Appay,
A.Brown,
T.Dudgeon,
L.A.Howard,
T.Meyers,
J.Owen,
S.R.Palan,
P.Tan,
G.Wilson,
N.R.Woods,
C.M.Heyworth,
B.I.Lord,
D.Brotherton,
R.Christison,
S.Craig,
S.Cribbes,
R.M.Edwards,
S.J.Evans,
R.Gilbert,
P.Morgan,
E.Randle,
N.Schofield,
P.G.Varley,
J.Fisher,
J.P.Waltho,
and
M.G.Hunter
(1999).
Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1alpha, MIP-1beta, and RANTES. Characterization of active disaggregated chemokine variants.
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J Biol Chem,
274,
16077-16084.
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PDB codes:
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J.S.Laurence,
A.C.LiWang,
and
P.J.LiWang
(1998).
Effect of N-terminal truncation and solution conditions on chemokine dimer stability: nuclear magnetic resonance structural analysis of macrophage inflammatory protein 1 beta mutants.
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Biochemistry,
37,
9346-9354.
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W.Shao,
L.F.Jerva,
J.West,
E.Lolis,
and
B.I.Schweitzer
(1998).
Solution structure of murine macrophage inflammatory protein-2.
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Biochemistry,
37,
8303-8313.
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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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