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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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2 terms
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Biological process
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immune response
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5 terms
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Biochemical function
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cytokine activity
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2 terms
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DOI no:
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Biochemistry
37:8303-8313
(1998)
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PubMed id:
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Solution structure of murine macrophage inflammatory protein-2.
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W.Shao,
L.F.Jerva,
J.West,
E.Lolis,
B.I.Schweitzer.
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ABSTRACT
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The solution structure of murine macrophage inflammatory protein-2 (MIP-2), a
heparin-binding chemokine that is secreted in response to inflammatory stimuli,
has been determined using two-dimensional homonuclear and heteronuclear NMR
spectroscopy. Structure calculations were carried out by means of torsion-angle
molecular dynamics using the program X-PLOR. The structure is based on a total
of 2390 experimental restraints, comprising 2246 NOE-derived distance
restraints, 44 distance restraints for 22 hydrogen bonds, and 100 torsion angle
restraints. The structure is well-defined, with the backbone (N, Calpha, C) and
heavy atom atomic rms distribution about the mean coordinates for residues 9-69
of the dimer being 0.57 +/- 0.16 A and 0.96 +/- 0.12 A, respectively. The N- and
C-terminal residues (1-8 and 70-73, respectively) are disordered. The overall
structure of the MIP-2 dimer is similar to that reported previously for the NMR
structures of MGSA and IL-8 and consists of a six-stranded antiparallel
beta-sheet (residue 25-29, 39-44, and 48-52) packed against two C-terminal
antiparallel alpha-helices. A best fit superposition of the NMR structure of
MIP-2 on the structures of MGSA, NAP-2, and the NMR and X-ray structures of IL-8
are 1.11, 1.02, 1.27, and 1.19 A, respectively, for the monomers, and 1.28,
1.10, 1.55, and 1.36 A, respectively, for the dimers (IL-8 residues 7-14 and
16-67, NAP-2 residues 25-84). At the tertiary level, the main differences
between the MIP-2 solution structure and the IL-8, MGSA, and NAP-2 structures
involve the N-terminal loop between residues 9-23 and the loops formed by
residues 30-38 and residues 53-58. At the quaternary level, the difference
between MIP-2 and IL-8, MGSA, or NAP-2 results from differing interhelical
angles and separations.
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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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J.Landsberg,
E.Gaffal,
M.Cron,
J.Kohlmeyer,
M.Renn,
and
T.Tüting
(2010).
Autochthonous primary and metastatic melanomas in Hgf-Cdk4 R24C mice evade T-cell-mediated immune surveillance.
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Pigment Cell Melanoma Res, 23,
649-660.
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J.Y.Springael,
E.Urizar,
and
M.Parmentier
(2005).
Dimerization of chemokine receptors and its functional consequences.
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Cytokine Growth Factor Rev, 16,
611-623.
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T.Schountz,
R.Green,
B.Davenport,
A.Buniger,
T.Richens,
J.J.Root,
F.Davidson,
C.H.Calisher,
and
B.J.Beaty
(2004).
Cloning and characterization of deer mouse (Peromyscus maniculatus) cytokine and chemokine cDNAs.
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BMC Immunol, 5,
1.
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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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K.Suetomi,
D.Rojo,
and
J.Navarro
(2002).
Identification of a signal transduction switch in the chemokine receptor CXCR1.
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J Biol Chem, 277,
31563-31566.
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W.Shao,
E.Fernandez,
A.Sachpatzidis,
J.Wilken,
D.A.Thompson,
B.I.Schweitzer,
and
E.Lolis
(2001).
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure.
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Eur J Biochem, 268,
2948-2959.
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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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T.Biedermann,
M.Kneilling,
R.Mailhammer,
K.Maier,
C.A.Sander,
G.Kollias,
S.L.Kunkel,
L.Hültner,
and
M.Röcken
(2000).
Mast cells control neutrophil recruitment during T cell-mediated delayed-type hypersensitivity reactions through tumor necrosis factor and macrophage inflammatory protein 2.
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J Exp Med, 192,
1441-1452.
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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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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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Links
