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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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1 term
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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
39:12837-12844
(2000)
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PubMed id:
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Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation.
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E.J.Fernandez,
J.Wilken,
D.A.Thompson,
S.C.Peiper,
E.Lolis.
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ABSTRACT
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Herpesvirus-8 macrophage inflammatory protein-II (vMIP-II) binds a uniquely wide
spectrum of chemokine receptors. We report the X-ray structure of vMIP-II
determined to 2.1 A resolution. Like RANTES, vMIP-II crystallizes as a dimer and
displays the conventional chemokine tertiary fold. We have compared the surface
topology and electrostatic potential of vMIP-II to those of eotaxin-1, RANTES,
and MCP-3, three CCR3 physiological agonists with known three-dimensional
structures. Surface epitopes identified on RANTES to be involved in binding to
CCR3 are mimicked on the eotaxin-1 and MCP-3 surface. However, the surface
topology of vMIP-II in these regions is markedly different. The results
presented here indicate that the structural basis for interaction with the
chemokine receptor CCR3 by vMIP-II is different from that for the physiological
agonists eotaxin-1, RANTES, and MCP-3. These differences on vMIP-II may be a
consequence of its broad-range receptor recognition capabilities.
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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.W.Murphy,
H.Yuan,
Y.Kong,
Y.Xiong,
and
E.J.Lolis
(2010).
Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family.
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Proteins, 78,
1331-1337.
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PDB codes:
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G.V.Crichlow,
H.Zhou,
H.H.Hsiao,
K.B.Frederick,
M.Debrosse,
Y.Yang,
E.J.Folta-Stogniew,
H.J.Chung,
C.Fan,
E.M.De la Cruz,
D.Levens,
E.Lolis,
and
D.Braddock
(2008).
Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c-myc inhibition.
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EMBO J, 27,
277-289.
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PDB code:
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D.Liu,
N.Madani,
Y.Li,
R.Cao,
W.T.Choi,
S.P.Kawatkar,
M.Y.Lim,
S.Kumar,
C.Z.Dong,
J.Wang,
J.D.Russell,
C.R.Lefebure,
J.An,
S.Wilson,
Y.G.Gao,
L.A.Pallansch,
J.G.Sodroski,
and
Z.Huang
(2007).
Crystal structure and structural mechanism of a novel anti-human immunodeficiency virus and D-amino acid-containing chemokine.
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J Virol, 81,
11489-11498.
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M.Miller-Kittrell,
J.Sai,
M.Penfold,
A.Richmond,
and
T.E.Sparer
(2007).
Functional characterization of chimpanzee cytomegalovirus chemokine, vCXCL-1(CCMV).
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Virology, 364,
454-465.
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Y.Li,
D.Liu,
R.Cao,
S.Kumar,
C.Dong,
J.An,
S.R.Wilson,
Y.G.Gao,
and
Z.Huang
(2007).
Crystal structure of chemically synthesized vMIP-II.
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Proteins, 67,
243-246.
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PDB codes:
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A.Jeshtadi,
G.Henriquet,
S.M.Laidlaw,
D.Hot,
Y.Zhang,
and
M.A.Skinner
(2005).
In vitro expression and analysis of secreted fowlpox virus CC chemokine-like proteins Fpv060, Fpv061, Fpv116 and Fpv121.
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Arch Virol, 150,
1745-1762.
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V.Petkovic,
C.Moghini,
S.Paoletti,
M.Uguccioni,
and
B.Gerber
(2004).
Eotaxin-3/CCL26 is a natural antagonist for CC chemokine receptors 1 and 5. A human chemokine with a regulatory role.
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J Biol Chem, 279,
23357-23363.
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E.J.Fernandez,
and
E.Lolis
(2002).
Structure, function, and inhibition of chemokines.
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Annu Rev Pharmacol Toxicol, 42,
469-499.
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M.Houimel,
P.Loetscher,
M.Baggiolini,
and
L.Mazzucchelli
(2001).
Functional inhibition of CCR3-dependent responses by peptides derived from phage libraries.
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Eur J Immunol, 31,
3535-3545.
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N.Zhou,
Z.Luo,
J.Luo,
D.Liu,
J.W.Hall,
R.J.Pomerantz,
and
Z.Huang
(2001).
Structural and functional characterization of human CXCR4 as a chemokine receptor and HIV-1 co-receptor by mutagenesis and molecular modeling studies.
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J Biol Chem, 276,
42826-42833.
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T.Rozmyslowicz,
J.Kijowski,
D.O.Conover,
M.Majka,
M.Baj-Krzyworzeka,
R.Reca,
J.J.Libura,
G.N.Gaulton,
and
M.Z.Ratajczak
(2001).
New T-lymphocytic cell lines for studying cell infectability by human immunodeficiency virus.
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Eur J Haematol, 67,
142-151.
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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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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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