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PDBsum entry 1esr
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* Residue conservation analysis
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DOI no:
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Biochemistry
39:14075-14081
(2000)
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PubMed id:
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Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors.
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J.Blaszczyk,
E.V.Coillie,
P.Proost,
J.V.Damme,
G.Opdenakker,
G.D.Bujacz,
J.M.Wang,
X.Ji.
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ABSTRACT
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Monocyte chemotactic protein 2 (MCP-2) is a CC chemokine that utilizes multiple
cellular receptors to attract and activate human leukocytes. MCP-2 is a potent
inhibitor of HIV-1 by virtue of its high-affinity binding to the receptor CCR5,
one of the major coreceptors for HIV-1. Although a few structures of CC
chemokines have been reported, none of these was determined with the N-terminal
pyroglutamic acid residue (pGlu1) and a complete C-terminus. pGlu1 is essential
for the chemotactic activity of MCP-2. Recombinant MCP-2 has Gln1 at the N
terminus, 12-15% of which cyclizes automatically and forms pGlu1. The
chemotactic activity of such MCP-2 mixture, which contains 12-15% pGlu1-form and
85-88% Gln1-form protein, is approximately 10 times lower when compared with
that of fully cyclized MCP-2 preparation. Therefore, this chemokine is
practically inactive without pGlu1. We have determined the complete crystal
structure of MCP-2 that contains both pGlu1 and an intact C-terminus. With the
existence of pGlu1, the conformation of the N-terminus allows two additional
interactions between the two subunits of MCP-2 dimer: a hydrogen bond between
pGlu1 and Asn17 and a salt bridge between Asp3 and Arg18. Consequently, both
pGlu1 are anchored and buried, and thereby, both N-terminal regions are
protected against protease degradation. We have also observed not previously
reported extended helical nature of the C terminal region, which covers residues
58-74.
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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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S.Cochran,
C.P.Li,
and
V.Ferro
(2009).
A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins.
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Glycoconj J,
26,
577-587.
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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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J.B.De Jesus,
P.Cuervo,
M.Junqueira,
C.Britto,
F.C.Silva-Filho,
L.Sabóia-Vahia,
L.J.González,
and
G.Barbosa Domont
(2007).
Application of two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for proteomic analysis of the sexually transmitted parasite Trichomonas vaginalis.
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J Mass Spectrom,
42,
1463-1473.
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S.J.Allen,
S.E.Crown,
and
T.M.Handel
(2007).
Chemokine: receptor structure, interactions, and antagonism.
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Annu Rev Immunol,
25,
787-820.
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J.S.Gillis
(2006).
Microarray evidence of glutaminyl cyclase gene expression in melanoma: implications for tumor antigen specific immunotherapy.
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J Transl Med,
4,
27.
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P.L.Arnold,
and
D.H.Fremont
(2006).
Structural determinants of chemokine binding by an Ectromelia virus-encoded decoy receptor.
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J Virol,
80,
7439-7449.
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PDB code:
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S.E.Crown,
Y.Yu,
M.D.Sweeney,
J.A.Leary,
and
T.M.Handel
(2006).
Heterodimerization of CCR2 chemokines and regulation by glycosaminoglycan binding.
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J Biol Chem,
281,
25438-25446.
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Y.Yu,
M.D.Sweeney,
O.M.Saad,
S.E.Crown,
A.R.Hsu,
T.M.Handel,
and
J.A.Leary
(2005).
Chemokine-glycosaminoglycan binding: specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry.
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J Biol Chem,
280,
32200-32208.
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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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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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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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