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PDBsum entry 1jpy
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Immune system
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PDB id
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1jpy
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Contents |
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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Crystal structure of il-17f
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Structure:
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Interleukin 17f. Chain: a, b, x, y. Fragment: secreted il-17f. Synonym: il-17f. Engineered: yes. Other_details: the first four residues, gshm, are from the vector
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: il-17f. Expressed in: unidentified baculovirus. Expression_system_taxid: 10469.
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Biol. unit:
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Tetramer (from
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Resolution:
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2.85Å
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R-factor:
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0.238
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R-free:
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0.284
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Authors:
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S.G.Hymowitz,E.H.Filvaroff,J.Yin,J.Lee,L.Cai,P.Risser,M.Maruoka, W.Mao,J.Foster,R.Kelley,G.Pan,A.L.Gurney,A.M.De Vos,M.A.Starovasnik
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Key ref:
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S.G.Hymowitz
et al.
(2001).
IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding.
EMBO J,
20,
5332-5341.
PubMed id:
DOI:
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Date:
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03-Aug-01
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Release date:
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28-Sep-01
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PROCHECK
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Headers
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References
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Q96PD4
(IL17F_HUMAN) -
Interleukin-17F from Homo sapiens
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Seq:
Struc:
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163 a.a.
121 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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EMBO J
20:5332-5341
(2001)
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PubMed id:
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IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding.
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S.G.Hymowitz,
E.H.Filvaroff,
J.P.Yin,
J.Lee,
L.Cai,
P.Risser,
M.Maruoka,
W.Mao,
J.Foster,
R.F.Kelley,
G.Pan,
A.L.Gurney,
A.M.de Vos,
M.A.Starovasnik.
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ABSTRACT
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The proinflammatory cytokine interleukin 17 (IL-17) is the founding member of a
family of secreted proteins that elicit potent cellular responses. We report a
novel human IL-17 homolog, IL-17F, and show that it is expressed by activated T
cells, can stimulate production of other cytokines such as IL-6, IL-8 and
granulocyte colony-stimulating factor, and can regulate cartilage matrix
turnover. Unexpectedly, the crystal structure of IL-17F reveals that IL-17
family members adopt a monomer fold typical of cystine knot growth factors,
despite lacking the disulfide responsible for defining the canonical
"knot" structure. IL-17F dimerizes in a parallel manner like
neurotrophins, and features an unusually large cavity on its surface.
Remarkably, this cavity is located in precisely the same position where nerve
growth factor binds its high affinity receptor, TrkA, suggesting further
parallels between IL-17s and neurotrophins with respect to receptor recognition.
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Selected figure(s)
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Figure 4.
Figure 4 The structure of IL-17F. (A) Ribbon trace of the IL-17F
monomer. Strands are labeled. Disulfides are shown as
ball-and-stick representation with the sulfur atoms colored
yellow. Glycosylation of Asn53 is indicated by a purple ball.
Inset shows a cartoon representation of the canonical cystine
knot fold. Cysteine residues are indicated by filled circles;
those present in IL-17 proteins are yellow, whereas the two that
are missing are black. (B) Ribbon trace of the IL-17F dimer.
Disulfides are shown as in (A). (C) The structure of NGF from
the NGF -TrkA complex (Wiesmann et al., 1999; Protein Data Bank
code 1WWW); a disordered loop connects strands 2 and 3.
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Figure 6.
Figure 6 Comparison of the IL-17F surface and the TrkA-binding
site on NGF. (A and B) The molecular surface of IL-17F is
oriented as in Figure 5. IL-17F is colored according to the
electrostatic surface potential: red, -5 kT; white, 0 kT; and
blue, +5 kT. The positions of the cavities are indicated by the
circles. (C) The molecular surface of NGF is shown in the same
orientation as IL-17F in (B) with the two protomers of the dimer
colored red and blue; domain 5 of TrkA is shown as a green
ribbon (Wiesmann et al., 1999).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
5332-5341)
copyright 2001.
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Figures were
selected
by the author.
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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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P.Miossec,
and
J.K.Kolls
(2012).
Targeting IL-17 and T(H)17 cells in chronic inflammation.
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Nat Rev Drug Discov,
11,
763-776.
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A.Puel,
S.Cypowyj,
J.Bustamante,
J.F.Wright,
L.Liu,
H.K.Lim,
M.Migaud,
L.Israel,
M.Chrabieh,
M.Audry,
M.Gumbleton,
A.Toulon,
C.Bodemer,
J.El-Baghdadi,
M.Whitters,
T.Paradis,
J.Brooks,
M.Collins,
N.M.Wolfman,
S.Al-Muhsen,
M.Galicchio,
L.Abel,
C.Picard,
and
J.L.Casanova
(2011).
Chronic mucocutaneous candidiasis in humans with inborn errors of interleukin-17 immunity.
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Science,
332,
65-68.
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M.Akdis,
S.Burgler,
R.Crameri,
T.Eiwegger,
H.Fujita,
E.Gomez,
S.Klunker,
N.Meyer,
L.O'Mahony,
O.Palomares,
C.Rhyner,
N.Quaked,
A.Schaffartzik,
W.Van De Veen,
S.Zeller,
M.Zimmermann,
and
C.A.Akdis
(2011).
Interleukins, from 1 to 37, and interferon-γ: receptors, functions, and roles in diseases.
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J Allergy Clin Immunol,
127,
701.
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N.Shen,
J.Wang,
M.Zhao,
F.Pei,
and
B.He
(2011).
Anti-interleukin-17 antibodies attenuate airway inflammation in tobacco-smoke-exposed mice.
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Inhal Toxicol,
23,
212-218.
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S.H.Chang,
and
C.Dong
(2011).
Signaling of interleukin-17 family cytokines in immunity and inflammation.
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Cell Signal,
23,
1069-1075.
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S.Kabir
(2011).
The role of interleukin-17 in the Helicobacter pylori induced infection and immunity.
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Helicobacter,
16,
1-8.
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X.Zhang,
P.Angkasekwinai,
C.Dong,
and
H.Tang
(2011).
Structure and function of interleukin-17 family cytokines.
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Protein Cell,
2,
26-40.
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Y.Chen,
P.Yang,
F.Li,
and
A.Kijlstra
(2011).
The effects of Th17 cytokines on the inflammatory mediator production and barrier function of ARPE-19 cells.
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PLoS One,
6,
e18139.
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Y.Hu,
F.Shen,
N.K.Crellin,
and
W.Ouyang
(2011).
The IL-17 pathway as a major therapeutic target in autoimmune diseases.
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Ann N Y Acad Sci,
1217,
60-76.
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Y.Iwakura,
H.Ishigame,
S.Saijo,
and
S.Nakae
(2011).
Functional specialization of interleukin-17 family members.
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Immunity,
34,
149-162.
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A.Paradowska-Gorycka,
E.Wojtecka-Lukasik,
J.Trefler,
B.Wojciechowska,
J.K.Lacki,
and
S.Maslinski
(2010).
Association between IL-17F gene polymorphisms and susceptibility to and severity of rheumatoid arthritis (RA).
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Scand J Immunol,
72,
134-141.
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A.W.Ho,
and
S.L.Gaffen
(2010).
IL-17RC: a partner in IL-17 signaling and beyond.
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Semin Immunopathol,
32,
33-42.
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C.Vock,
H.P.Hauber,
and
M.Wegmann
(2010).
The other T helper cells in asthma pathogenesis.
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J Allergy (Cairo),
2010,
519298.
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E.Lubberts
(2010).
Th17 cytokines and arthritis.
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Semin Immunopathol,
32,
43-53.
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H.Nakajima,
and
K.Hirose
(2010).
Role of IL-23 and Th17 Cells in Airway Inflammation in Asthma.
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Immune Netw,
10,
1-4.
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J.F.Alcorn,
C.R.Crowe,
and
J.K.Kolls
(2010).
TH17 cells in asthma and COPD.
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Annu Rev Physiol,
72,
495-516.
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J.M.Reynolds,
P.Angkasekwinai,
and
C.Dong
(2010).
IL-17 family member cytokines: regulation and function in innate immunity.
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Cytokine Growth Factor Rev,
21,
413-423.
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M.L.Toh,
G.Gonzales,
M.I.Koenders,
A.Tournadre,
D.Boyle,
E.Lubberts,
Y.Zhou,
G.S.Firestein,
W.B.van den Berg,
and
P.Miossec
(2010).
Role of interleukin 17 in arthritis chronicity through survival of synoviocytes via regulation of synoviolin expression.
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PLoS One,
5,
e13416.
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P.L.Simonian,
F.Wehrmann,
C.L.Roark,
W.K.Born,
R.L.O'Brien,
and
A.P.Fontenot
(2010).
γδ T cells protect against lung fibrosis via IL-22.
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J Exp Med,
207,
2239-2253.
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R.H.Prabhala,
D.Pelluru,
M.Fulciniti,
H.K.Prabhala,
P.Nanjappa,
W.Song,
C.Pai,
S.Amin,
Y.T.Tai,
P.G.Richardson,
I.M.Ghobrial,
S.P.Treon,
J.F.Daley,
K.C.Anderson,
J.L.Kutok,
and
N.C.Munshi
(2010).
Elevated IL-17 produced by TH17 cells promotes myeloma cell growth and inhibits immune function in multiple myeloma.
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Blood,
115,
5385-5392.
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R.Pappu,
V.Ramirez-Carrozzi,
N.Ota,
W.Ouyang,
and
Y.Hu
(2010).
The IL-17 family cytokines in immunity and disease.
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J Clin Immunol,
30,
185-195.
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S.Xu,
and
X.Cao
(2010).
Interleukin-17 and its expanding biological functions.
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Cell Mol Immunol,
7,
164-174.
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Y.Qian,
Z.Kang,
C.Liu,
and
X.Li
(2010).
IL-17 signaling in host defense and inflammatory diseases.
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Cell Mol Immunol,
7,
328-333.
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Y.Xie,
W.Sheng,
J.Xiang,
Z.Ye,
and
J.Yang
(2010).
Interleukin-17F suppresses hepatocarcinoma cell growth via inhibition of tumor angiogenesis.
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Cancer Invest,
28,
598-607.
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B.R.Marks,
and
J.Craft
(2009).
Barrier immunity and IL-17.
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Semin Immunol,
21,
164-171.
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H.Ishigame,
S.Kakuta,
T.Nagai,
M.Kadoki,
A.Nambu,
Y.Komiyama,
N.Fujikado,
Y.Tanahashi,
A.Akitsu,
H.Kotaki,
K.Sudo,
S.Nakae,
C.Sasakawa,
and
Y.Iwakura
(2009).
Differential roles of interleukin-17A and -17F in host defense against mucoepithelial bacterial infection and allergic responses.
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Immunity,
30,
108-119.
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H.Watanabe,
M.Kawaguchi,
S.Fujishima,
M.Ogura,
S.Matsukura,
H.Takeuchi,
M.Ohba,
H.Sueki,
F.Kokubu,
N.Hizawa,
M.Adachi,
S.K.Huang,
and
M.Iijima
(2009).
Functional characterization of IL-17F as a selective neutrophil attractant in psoriasis.
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J Invest Dermatol,
129,
650-656.
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L.K.Ely,
S.Fischer,
and
K.C.Garcia
(2009).
Structural basis of receptor sharing by interleukin 17 cytokines.
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Nat Immunol,
10,
1245-1251.
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PDB code:
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M.Kawaguchi,
J.Fujita,
F.Kokubu,
S.K.Huang,
T.Homma,
S.Matsukura,
M.Adachi,
and
N.Hizawa
(2009).
IL-17F-induced IL-11 release in bronchial epithelial cells via MSK1-CREB pathway.
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Am J Physiol Lung Cell Mol Physiol,
296,
L804-L810.
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R.Gras,
L.Almonacid,
P.Ortega,
M.J.Serramia,
R.Gomez,
F.J.de la Mata,
L.A.Lopez-Fernandez,
and
M.A.Muñoz-Fernandez
(2009).
Changes in gene expression pattern of human primary macrophages induced by carbosilane dendrimer 2G-NN16.
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Pharm Res,
26,
577-586.
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S.H.Chang,
and
C.Dong
(2009).
IL-17F: regulation, signaling and function in inflammation.
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Cytokine,
46,
7.
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S.Haak,
A.L.Croxford,
K.Kreymborg,
F.L.Heppner,
S.Pouly,
B.Becher,
and
A.Waisman
(2009).
IL-17A and IL-17F do not contribute vitally to autoimmune neuro-inflammation in mice.
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J Clin Invest,
119,
61-69.
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S.Ivanov,
and
A.Lindén
(2009).
Interleukin-17 as a drug target in human disease.
|
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Trends Pharmacol Sci,
30,
95.
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S.L.Gaffen
(2009).
Structure and signalling in the IL-17 receptor family.
|
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Nat Rev Immunol,
9,
556-567.
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S.Yehuda,
B.Sredni,
R.L.Carasso,
and
D.Kenigsbuch-Sredni
(2009).
REM sleep deprivation in rats results in inflammation and interleukin-17 elevation.
|
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J Interferon Cytokine Res,
29,
393-398.
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S.von Vietinghoff,
and
K.Ley
(2009).
IL-17A controls IL-17F production and maintains blood neutrophil counts in mice.
|
| |
J Immunol,
183,
865-873.
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T.Korn,
E.Bettelli,
M.Oukka,
and
V.K.Kuchroo
(2009).
IL-17 and Th17 Cells.
|
| |
Annu Rev Immunol,
27,
485-517.
|
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|
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|
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V.Veverka,
A.J.Henry,
P.M.Slocombe,
A.Ventom,
B.Mulloy,
F.W.Muskett,
M.Muzylak,
K.Greenslade,
A.Moore,
L.Zhang,
J.Gong,
X.Qian,
C.Paszty,
R.J.Taylor,
M.K.Robinson,
and
M.D.Carr
(2009).
Characterization of the Structural Features and Interactions of Sclerostin: MOLECULAR INSIGHT INTO A KEY REGULATOR OF Wnt-MEDIATED BONE FORMATION.
|
| |
J Biol Chem,
284,
10890-10900.
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PDB code:
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W.Ouyang,
E.Filvaroff,
Y.Hu,
and
J.Grogan
(2009).
Novel therapeutic targets along the Th17 pathway.
|
| |
Eur J Immunol,
39,
670-675.
|
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|
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Y.K.Lee,
H.Turner,
C.L.Maynard,
J.R.Oliver,
D.Chen,
C.O.Elson,
and
C.T.Weaver
(2009).
Late developmental plasticity in the T helper 17 lineage.
|
| |
Immunity,
30,
92.
|
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|
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B.P.Pappu,
P.Angkasekwinai,
and
C.Dong
(2008).
Regulatory mechanisms of helper T cell differentiation: new lessons learned from interleukin 17 family cytokines.
|
| |
Pharmacol Ther,
117,
374-384.
|
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|
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|
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C.Dong
(2008).
TH17 cells in development: an updated view of their molecular identity and genetic programming.
|
| |
Nat Rev Immunol,
8,
337-348.
|
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|
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E.Bettelli,
T.Korn,
M.Oukka,
and
V.K.Kuchroo
(2008).
Induction and effector functions of T(H)17 cells.
|
| |
Nature,
453,
1051-1057.
|
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|
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F.Shen,
and
S.L.Gaffen
(2008).
Structure-function relationships in the IL-17 receptor: implications for signal transduction and therapy.
|
| |
Cytokine,
41,
92.
|
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J.Zhang,
P.D.Paré,
and
A.J.Sandford
(2008).
Recent advances in asthma genetics.
|
| |
Respir Res,
9,
4.
|
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|
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|
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J.Zhu,
and
W.E.Paul
(2008).
CD4 T cells: fates, functions, and faults.
|
| |
Blood,
112,
1557-1569.
|
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L.A.Garrett-Sinha,
S.John,
and
S.L.Gaffen
(2008).
IL-17 and the Th17 lineage in systemic lupus erythematosus.
|
| |
Curr Opin Rheumatol,
20,
519-525.
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M.Garley,
and
E.Jablonska
(2008).
Chosen IL-17 family proteins in neutrophils of patients with oral inflammation.
|
| |
Adv Med Sci,
53,
326-330.
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S.A.Saenz,
B.C.Taylor,
and
D.Artis
(2008).
Welcome to the neighborhood: epithelial cell-derived cytokines license innate and adaptive immune responses at mucosal sites.
|
| |
Immunol Rev,
226,
172-190.
|
|
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|
|
|
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S.L.Gaffen
(2008).
An overview of IL-17 function and signaling.
|
| |
Cytokine,
43,
402-407.
|
|
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|
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|
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S.L.Gaffen,
and
G.Hajishengallis
(2008).
A new inflammatory cytokine on the block: re-thinking periodontal disease and the Th1/Th2 paradigm in the context of Th17 cells and IL-17.
|
| |
J Dent Res,
87,
817-828.
|
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|
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T.Kokubu,
D.R.Haudenschild,
T.A.Moseley,
L.Rose,
and
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PDB codes:
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
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