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PDBsum entry 1j0s
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* Residue conservation analysis
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PDB id:
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Cytokine
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Title:
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Solution structure of the human interleukin-18
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Structure:
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Interleukin-18. Chain: a. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
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NMR struc:
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20 models
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Authors:
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Z.Kato,J.Jee,H.Shikano,M.Mishima,I.Ohki,T.Yoneda,T.Hara,K.Torigoe, N.Kondo,M.Shirakawa
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Key ref:
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Z.Kato
et al.
(2003).
The structure and binding mode of interleukin-18.
Nat Struct Biol,
10,
966-971.
PubMed id:
DOI:
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Date:
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21-Nov-02
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Release date:
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11-Nov-03
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PROCHECK
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Headers
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References
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Q14116
(IL18_HUMAN) -
Interleukin-18 from Homo sapiens
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Seq:
Struc:
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193 a.a.
157 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Nat Struct Biol
10:966-971
(2003)
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PubMed id:
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The structure and binding mode of interleukin-18.
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Z.Kato,
J.Jee,
H.Shikano,
M.Mishima,
I.Ohki,
H.Ohnishi,
A.Li,
K.Hashimoto,
E.Matsukuma,
K.Omoya,
Y.Yamamoto,
T.Yoneda,
T.Hara,
N.Kondo,
M.Shirakawa.
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ABSTRACT
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Interleukin-18 (IL-18), a cytokine formerly known as interferon-gamma-
(IFN-gamma-) inducing factor, has pleiotropic immunoregulatory functions,
including augmentation of IFN-gamma production, Fas-mediated cytotoxicity and
developmental regulation of T-lymphocyte helper type I. We determined the
solution structure of IL-18 as a first step toward understanding its receptor
activation mechanism. It folds into a beta-trefoil structure that resembles that
of IL-1. Extensive mutagenesis revealed the presence of three sites that are
important for receptor activation: two serve as binding sites for IL-18 receptor
alpha (IL-18Ralpha), located at positions similar to those of IL-1 for IL-1
receptor type I (IL-1RI), whereas the third site may be involved in IL-18
receptor beta (IL-18Rbeta) binding. The structure and mutagenesis data provide a
basis for understanding the IL-18-induced heterodimerization of receptor
subunits, which is necessary for receptor activation.
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Selected figure(s)
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Figure 1.
Figure 1. Solution structure of human IL-18. (a) Stereo view
of the best-fit backbone superposition of the 20 final
structures. The backbone atoms of residues 1 -157 are
superimposed. (b) Schematic ribbon drawing of the NMR structure
of IL-18, drawn with MolMol30.
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Figure 3.
Figure 3. Models for the complex of IL-18 and IL-18R  ,
and interactions among IL-18, IL-18R and
IL-18R  .
(a) Crystal structure of the complex of IL-1  and
IL-1RI (PDB entry 1ITB). IL-1 residues
in sites A and B are red and orange, respectively. (b) Modeled
structure of the complex of IL-18 and IL-18R  .
IL-18 residues in sites I, II and III are red, orange and blue,
respectively. In a and b, the molecule on the right is viewed as
rotated by 90° about the vertical axis relative to the image on
the left. (c) Dose-response curves of surface plasmon resonance
for wild-type IL-18 to immobilized IL-18R or
to immobilized IL-18R .
Concentration of wild-type IL-18 is also indicated. (d) Response
curves of surface plasmon resonance for IL-18R for
to the complex of immobilized IL-18R with
wild-type IL-18 or the site III mutant proteins.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
966-971)
copyright 2003.
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Figures were
selected
by an automated process.
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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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D.Wang,
S.Zhang,
L.Li,
X.Liu,
K.Mei,
and
X.Wang
(2010).
Structural insights into the assembly and activation of IL-1β with its receptors.
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Nat Immunol,
11,
905-911.
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PDB code:
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M.Trøseid,
I.Seljeflot,
and
H.Arnesen
(2010).
The role of interleukin-18 in the metabolic syndrome.
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Cardiovasc Diabetol,
9,
11.
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A.Lingel,
T.M.Weiss,
M.Niebuhr,
B.Pan,
B.A.Appleton,
C.Wiesmann,
J.F.Bazan,
and
W.J.Fairbrother
(2009).
Structure of IL-33 and its interaction with the ST2 and IL-1RAcP receptors--insight into heterotrimeric IL-1 signaling complexes.
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Structure,
17,
1398-1410.
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PDB code:
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M.A.Argiriadi,
T.Xiang,
C.Wu,
T.Ghayur,
and
D.W.Borhani
(2009).
Unusual water-mediated antigenic recognition of the proinflammatory cytokine interleukin-18.
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J Biol Chem,
284,
24478-24489.
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PDB codes:
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M.L.Grisoni,
C.Proust,
M.Alanne,
M.Desuremain,
V.Salomaa,
K.Kuulasmaa,
F.Cambien,
V.Nicaud,
P.G.Wiklund,
J.Virtamo,
F.Kee,
L.Tiret,
A.Evans,
and
D.A.Tregouet
(2009).
Lack of association between polymorphisms of the IL18R1 and IL18RAP genes and cardiovascular risk: the MORGAM Project.
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BMC Med Genet,
10,
44.
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S.Alboni,
D.Cervia,
B.Ross,
C.Montanari,
A.S.Gonzalez,
M.Sanchez-Alavez,
M.C.Marcondes,
D.De Vries,
S.Sugama,
N.Brunello,
J.Blom,
F.Tascedda,
and
B.Conti
(2009).
Mapping of the full length and the truncated interleukin-18 receptor alpha in the mouse brain.
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J Neuroimmunol,
214,
43-54.
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S.W.Rabkin
(2009).
The role of interleukin 18 in the pathogenesis of hypertension-induced vascular disease.
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Nat Clin Pract Cardiovasc Med,
6,
192-199.
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W.de Jager,
S.J.Vastert,
J.M.Beekman,
N.M.Wulffraat,
W.Kuis,
P.J.Coffer,
and
B.J.Prakken
(2009).
Defective phosphorylation of interleukin-18 receptor beta causes impaired natural killer cell function in systemic-onset juvenile idiopathic arthritis.
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Arthritis Rheum,
60,
2782-2793.
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B.Krumm,
X.Meng,
Y.Li,
Y.Xiang,
and
J.Deng
(2008).
Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein.
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Proc Natl Acad Sci U S A,
105,
20711-20715.
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PDB code:
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S.Gosavi,
P.C.Whitford,
P.A.Jennings,
and
J.N.Onuchic
(2008).
Extracting function from a beta-trefoil folding motif.
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Proc Natl Acad Sci U S A,
105,
10384-10389.
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S.H.Nazarian,
M.M.Rahman,
S.J.Werden,
D.Villeneuve,
X.Meng,
C.Brunetti,
C.Valeriano,
C.Wong,
R.Singh,
J.W.Barrett,
Y.Xiang,
and
G.McFadden
(2008).
Yaba monkey tumor virus encodes a functional inhibitor of interleukin-18.
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J Virol,
82,
522-528.
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T.Kimura,
Z.Kato,
H.Ohnishi,
H.Tochio,
M.Shirakawa,
and
N.Kondo
(2008).
Expression, purification and structural analysis of human IL-18 binding protein: a potent therapeutic molecule for allergy.
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Allergol Int,
57,
367-376.
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D.Montufar-Solis,
T.Garza,
and
J.R.Klein
(2007).
T-cell activation in the intestinal mucosa.
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Immunol Rev,
215,
189-201.
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E.J.Anderson,
M.A.McGrath,
T.Thalhamer,
and
I.B.McInnes
(2006).
Interleukin-12 to interleukin 'infinity': the rationale for future therapeutic cytokine targeting.
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Springer Semin Immunopathol,
27,
425-442.
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E.Matsukuma,
Z.Kato,
K.Omoya,
K.Hashimoto,
A.Li,
Y.Yamamoto,
H.Ohnishi,
H.Hiranuma,
H.Komine,
and
N.Kondo
(2006).
Development of fluorescence-linked immunosorbent assay for high throughput screening of interferon-gamma.
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Allergol Int,
55,
49-54.
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H.Kaneko,
E.Matsui,
T.Asano,
Z.Kato,
T.Teramoto,
M.Aoki,
N.Kawamoto,
L.A.Lian,
K.Kasahara,
and
N.Kondo
(2006).
Suppression of IFN-gamma production in atopic group at the acute phase of RSV infection.
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Pediatr Allergy Immunol,
17,
370-375.
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C.A.Dinarello,
and
G.Kaplanski
(2005).
Interleukin-18 treatment options for inflammatory diseases.
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Expert Rev Clin Immunol,
1,
619-632.
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K.Fukushima,
Y.Ikehara,
and
K.Yamashita
(2005).
Functional role played by the glycosylphosphatidylinositol anchor glycan of CD48 in interleukin-18-induced interferon-gamma production.
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J Biol Chem,
280,
18056-18062.
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M.Hosamani,
B.Mondal,
Y.Muneta,
and
T.J.Rasool
(2005).
Molecular characterization and expression of caprine (Capra hircus) interleukin-18 cDNA.
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Int J Immunogenet,
32,
293-297.
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R.L.Rich,
and
D.G.Myszka
(2005).
Survey of the year 2003 commercial optical biosensor literature.
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J Mol Recognit,
18,
1.
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S.H.Kim,
S.Y.Han,
T.Azam,
D.Y.Yoon,
and
C.A.Dinarello
(2005).
Interleukin-32: a cytokine and inducer of TNFalpha.
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Immunity,
22,
131-142.
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Y.J.Yang,
Z.Y.Wang,
S.H.Chen,
and
X.R.Ge
(2005).
Cloning and characterization of a new isoform of mouse interleukin-18.
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Acta Biochim Biophys Sin (Shanghai),
37,
826-834.
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H.Tsutsui,
T.Yoshimoto,
N.Hayashi,
H.Mizutani,
and
K.Nakanishi
(2004).
Induction of allergic inflammation by interleukin-18 in experimental animal models.
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Immunol Rev,
202,
115-138.
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J.Zou,
S.Bird,
J.Truckle,
N.Bols,
M.Horne,
and
C.Secombes
(2004).
Identification and expression analysis of an IL-18 homologue and its alternatively spliced form in rainbow trout (Oncorhynchus mykiss).
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Eur J Biochem,
271,
1913-1923.
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P.Reddy
(2004).
Interleukin-18: recent advances.
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Curr Opin Hematol,
11,
405-410.
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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
