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* Residue conservation analysis
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J Biol Chem
264:2092-2099
(1989)
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PubMed id:
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The three-dimensional structure of bovine platelet factor 4 at 3.0-A resolution.
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R.St Charles,
D.A.Walz,
B.F.Edwards.
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ABSTRACT
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Platelet factor 4 (PF4), which is released by platelets during coagulation,
binds very tightly to negatively charged oligosaccharides such as heparin. To
date, six other proteins are known that are homologous in sequence with PF4 but
have quite different functions. The structure of a tetramer of bovine PF4
complexed with one Ni(CN)4(2-) molecule has been determined at 3.0 A resolution
and refined to an R factor of 0.28. The current model contains residues 24-85,
no solvent, and one overall temperature factor. Residues 1-13, which carried an
oligosaccharide chain, were removed with elastase to induce crystallization;
residues 14-23 and presumably 86-88 are disordered in the electron density map.
Because no heavy atom derivative was isomorphous with the native crystals, the
complex of PF4 with one Ni(CN)4(2-) molecule was solved using a single, highly
isomorphous Pt(CN)4(2-) derivative and the iterative, single isomorphous
replacement method. The secondary structure of the PF4 subunit, from amino- to
carboxyl-terminal end, consists of an extended loop, three strands of
antiparallel beta-sheet arranged in a Greek key, and one alpha-helix. The
tetramer contains two extended, six-stranded beta-sheets, each formed by two
subunits, which are arranged back-to-back to form a "beta-bilayer" structure
with two buried salt bridges sandwiched in the middle. The carboxyl-terminal
alpha-helices, which contain lysine residues that are thought to be intimately
involved in binding heparin, are arranged as antiparallel pairs on the surface
of each extended beta-sheet.
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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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PDB code:
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PDB code:
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Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
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Biochemistry,
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PDB code:
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G.S.Kuschert,
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Identification of a glycosaminoglycan binding surface on human interleukin-8.
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Biochemistry,
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W.Shao,
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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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J.Lubkowski,
G.Bujacz,
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The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions.
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Nat Struct Biol,
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PDB codes:
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L.F.Jerva,
G.Sullivan,
and
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Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: sequence analysis and mutagenesis identify receptor binding epitopes.
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Protein Sci,
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Annu Rev Immunol,
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S.Meunier,
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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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Biochemistry,
36,
4412-4422.
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PDB code:
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E.E.Caldwell,
V.D.Nadkarni,
J.R.Fromm,
R.J.Linhardt,
and
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(1996).
Importance of specific amino acids in protein binding sites for heparin and heparan sulfate.
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Int J Biochem Cell Biol,
28,
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K.H.Mayo,
E.Ilyina,
and
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Protein Sci,
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A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4.
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Proc Natl Acad Sci U S A,
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gro-beta, a -C-X-C- chemokine, is an angiogenesis inhibitor that suppresses the growth of Lewis lung carcinoma in mice.
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and
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A dominant negative inhibitor indicates that monocyte chemoattractant protein 1 functions as a dimer.
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Mol Cell Biol,
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D.G.Covell,
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Protein Sci,
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D.P.Witt,
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Curr Biol,
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A.Andalibi,
L.Chaverri-Almada,
J.A.Berliner,
T.Kirchgessner,
Z.T.Fang,
P.Tekamp-Olson,
A.J.Lusis,
C.Gallegos,
and
A.M.Fogelman
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Role of the GRO family of chemokines in monocyte adhesion to MM-LDL-stimulated endothelium.
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J Clin Invest,
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G.P.Visentin,
S.E.Ford,
J.P.Scott,
and
R.H.Aster
(1994).
Antibodies from patients with heparin-induced thrombocytopenia/thrombosis are specific for platelet factor 4 complexed with heparin or bound to endothelial cells.
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J Clin Invest,
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J.N.Heinrich,
E.C.O'Rourke,
L.Chen,
H.Gray,
K.S.Dorfman,
and
R.Bravo
(1994).
Biological activity of the growth factor-induced cytokine N51: structure-function analysis using N51/Interleukin-8 chimeric molecules.
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Mol Cell Biol,
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P.Sinnis,
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Structural and functional properties of region II-plus of the malaria circumsporozoite protein.
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C.J.Talpas,
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Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes.
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I.Clark-Lewis,
B.Dewald,
T.Geiser,
B.Moser,
and
M.Baggiolini
(1993).
Platelet factor 4 binds to interleukin 8 receptors and activates neutrophils when its N terminus is modified with Glu-Leu-Arg.
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Proc Natl Acad Sci U S A,
90,
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I.Clark-Lewis,
M.Baggiolini,
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Binding to heparan sulfate or heparin enhances neutrophil responses to interleukin 8.
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PDB code:
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PDB codes:
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P.Tekamp-Olson,
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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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