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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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3 terms
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Biological process
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negative regulation of growth of symbiont in host
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51 terms
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Biochemical function
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cytokine activity
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3 terms
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DOI no:
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Biochemistry
34:12118-12125
(1995)
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PubMed id:
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Crystal structure of interleukin 10 reveals an interferon gamma-like fold.
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M.R.Walter,
T.L.Nagabhushan.
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ABSTRACT
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The crystal structure of recombinant human interleukin 10 (rhIL-10) has been
determined by X-ray crystallography at 2.0 A resolution. Interleukin 10 is a
dimer composed of identical polypeptide chains related by a 2-fold axis. The
molecule is predominantly alpha-helical. The main-chain fold resembles that of
interferon gamma (IFN-gamma) in which the structural integrity of each domain is
dependent on the intertwining of helices from each peptide chain. Comparison of
rhIL-10 and IFN-gamma reveals differences in helix lengths and orientations of
the 2-fold related domains. Interleukin 10 and IFN-gamma contain several
conserved residues in their internal cores which suggest a possible
"fingerprint" for detection of other members of this fold.
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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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W.Ouyang,
S.Rutz,
N.K.Crellin,
P.A.Valdez,
and
S.G.Hymowitz
(2011).
Regulation and functions of the IL-10 family of cytokines in inflammation and disease.
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Annu Rev Immunol, 29,
71.
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A.Zdanov
(2010).
Structural analysis of cytokines comprising the IL-10 family.
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Cytokine Growth Factor Rev, 21,
325-330.
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D.B.Trivella,
J.R.Ferreira-Júnior,
L.Dumoutier,
J.C.Renauld,
and
I.Polikarpov
(2010).
Structure and function of interleukin-22 and other members of the interleukin-10 family.
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Cell Mol Life Sci, 67,
2909-2935.
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H.H.Gad,
O.J.Hamming,
and
R.Hartmann
(2010).
The structure of human interferon lambda and what it has taught us.
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J Interferon Cytokine Res, 30,
565-571.
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R.P.Donnelly,
F.Sheikh,
H.Dickensheets,
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H.A.Young,
and
M.R.Walter
(2010).
Interleukin-26: an IL-10-related cytokine produced by Th17 cells.
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Cytokine Growth Factor Rev, 21,
393-401.
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R.Sabat
(2010).
IL-10 family of cytokines.
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Cytokine Growth Factor Rev, 21,
315-324.
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R.Sabat,
G.Grütz,
K.Warszawska,
S.Kirsch,
E.Witte,
K.Wolk,
and
J.Geginat
(2010).
Biology of interleukin-10.
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Cytokine Growth Factor Rev, 21,
331-344.
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U.M.Wegenka
(2010).
IL-20: biological functions mediated through two types of receptor complexes.
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Cytokine Growth Factor Rev, 21,
353-363.
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B.C.Jones,
N.J.Logsdon,
and
M.R.Walter
(2008).
Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to the extracellular IL-22R1 chain.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 64,
266-269.
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B.C.Jones,
N.J.Logsdon,
and
M.R.Walter
(2008).
Structure of IL-22 bound to its high-affinity IL-22R1 chain.
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Structure, 16,
1333-1344.
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PDB code:
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C.Jenkins,
W.Garcia,
M.J.Godwin,
J.V.Spencer,
J.L.Stern,
A.Abendroth,
and
B.Slobedman
(2008).
Immunomodulatory properties of a viral homolog of human interleukin-10 expressed by human cytomegalovirus during the latent phase of infection.
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J Virol, 82,
3736-3750.
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M.de Oliveira Neto,
J.R.Ferreira,
D.Colau,
H.Fischer,
A.S.Nascimento,
A.F.Craievich,
L.Dumoutier,
J.C.Renauld,
and
I.Polikarpov
(2008).
Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains.
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Biophys J, 94,
1754-1765.
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W.Li,
A.Lewis-Antes,
J.Huang,
M.Balan,
and
S.V.Kotenko
(2008).
Regulation of apoptosis by type III interferons.
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Cell Prolif, 41,
960-979.
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S.I.Yoon,
and
M.R.Walter
(2007).
Identification and characterization of a +1 frameshift observed during the expression of Epstein-Barr virus IL-10 in Escherichia coli.
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Protein Expr Purif, 53,
132-137.
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K.Wolk,
and
R.Sabat
(2006).
Interleukin-22: a novel T- and NK-cell derived cytokine that regulates the biology of tissue cells.
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Cytokine Growth Factor Rev, 17,
367-380.
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S.I.Yoon,
B.C.Jones,
N.J.Logsdon,
and
M.R.Walter
(2005).
Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain.
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Structure, 13,
551-564.
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PDB codes:
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S.Pletnev,
E.Magracheva,
A.Wlodawer,
and
A.Zdanov
(2005).
A model of the ternary complex of interleukin-10 with its soluble receptors.
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BMC Struct Biol, 5,
10.
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T.Xu,
N.J.Logsdon,
and
M.R.Walter
(2005).
Structure of insect-cell-derived IL-22.
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Acta Crystallogr D Biol Crystallogr, 61,
942-950.
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PDB code:
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S.Pestka,
C.D.Krause,
D.Sarkar,
M.R.Walter,
Y.Shi,
and
P.B.Fisher
(2004).
Interleukin-10 and related cytokines and receptors.
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Annu Rev Immunol, 22,
929-979.
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T.Xu,
N.J.Logsdon,
and
M.R.Walter
(2004).
Crystallization and X-ray diffraction analysis of insect-cell-derived IL-22.
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Acta Crystallogr D Biol Crystallogr, 60,
1295-1298.
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C.Chang,
E.Magracheva,
S.Kozlov,
S.Fong,
G.Tobin,
S.Kotenko,
A.Wlodawer,
and
A.Zdanov
(2003).
Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.
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J Biol Chem, 278,
3308-3313.
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PDB code:
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G.Lutfalla,
H.Roest Crollius,
N.Stange-Thomann,
O.Jaillon,
K.Mogensen,
and
D.Monneron
(2003).
Comparative genomic analysis reveals independent expansion of a lineage-specific gene family in vertebrates: the class II cytokine receptors and their ligands in mammals and fish.
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BMC Genomics, 4,
29.
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J.C.Renauld
(2003).
Class II cytokine receptors and their ligands: key antiviral and inflammatory modulators.
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Nat Rev Immunol, 3,
667-676.
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B.C.Jones,
N.J.Logsdon,
K.Josephson,
J.Cook,
P.A.Barry,
and
M.R.Walter
(2002).
Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1.
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Proc Natl Acad Sci U S A, 99,
9404-9409.
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PDB code:
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H.Fickenscher,
S.Hör,
H.Küpers,
A.Knappe,
S.Wittmann,
and
H.Sticht
(2002).
The interleukin-10 family of cytokines.
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Trends Immunol, 23,
89-96.
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K.Josephson,
B.C.Jones,
L.J.Walter,
R.DiGiacomo,
S.R.Indelicato,
and
M.R.Walter
(2002).
Noncompetitive antibody neutralization of IL-10 revealed by protein engineering and x-ray crystallography.
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Structure, 10,
981-987.
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PDB code:
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K.Vandenbroeck,
I.Alloza,
D.Brehmer,
A.Billiau,
P.Proost,
N.McFerran,
S.Rüdiger,
and
B.Walker
(2002).
The conserved helix C region in the superfamily of interferon-gamma /interleukin-10-related cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK.
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J Biol Chem, 277,
25668-25676.
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N.J.Logsdon,
B.C.Jones,
K.Josephson,
J.Cook,
and
M.R.Walter
(2002).
Comparison of interleukin-22 and interleukin-10 soluble receptor complexes.
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J Interferon Cytokine Res, 22,
1099-1112.
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S.V.Kotenko
(2002).
The family of IL-10-related cytokines and their receptors: related, but to what extent?
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Cytokine Growth Factor Rev, 13,
223-240.
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K.Josephson,
D.T.McPherson,
and
M.R.Walter
(2001).
Purification, crystallization and preliminary X-ray diffraction of a complex between IL-10 and soluble IL-10R1.
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Acta Crystallogr D Biol Crystallogr, 57,
1908-1911.
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K.W.Moore,
R.de Waal Malefyt,
R.L.Coffman,
and
A.O'Garra
(2001).
Interleukin-10 and the interleukin-10 receptor.
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Annu Rev Immunol, 19,
683-765.
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M.Randal,
and
A.A.Kossiakoff
(2001).
The structure and activity of a monomeric interferon-gamma:alpha-chain receptor signaling complex.
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Structure, 9,
155-163.
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PDB code:
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K.Asadullah,
W.D.Döcke,
R.V.Sabat,
H.D.Volk,
and
W.Sterry
(2000).
The treatment of psoriasis with IL-10: rationale and review of the first clinical trials.
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Expert Opin Investig Drugs, 9,
95.
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K.Josephson,
R.DiGiacomo,
S.R.Indelicato,
A.H.Iyo,
T.L.Nagabhushan,
M.H.Parker,
M.R.Walter,
and
A.H.Ayo
(2000).
Design and analysis of an engineered human interleukin-10 monomer.
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J Biol Chem, 275,
13552-13557.
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M.Randal,
and
A.A.Kossiakoff
(2000).
The 2.0 A structure of bovine interferon-gamma; assessment of the structural differences between species.
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Acta Crystallogr D Biol Crystallogr, 56,
14-24.
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PDB codes:
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S.V.Kotenko,
S.Saccani,
L.S.Izotova,
O.V.Mirochnitchenko,
and
S.Pestka
(2000).
Human cytomegalovirus harbors its own unique IL-10 homolog (cmvIL-10).
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Proc Natl Acad Sci U S A, 97,
1695-1700.
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Y.Ding,
L.Qin,
S.V.Kotenko,
S.Pestka,
and
J.S.Bromberg
(2000).
A single amino acid determines the immunostimulatory activity of interleukin 10.
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J Exp Med, 191,
213-224.
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D.M.Hoover,
C.Schalk-Hihi,
C.C.Chou,
S.Menon,
A.Wlodawer,
and
A.Zdanov
(1999).
Purification of receptor complexes of interleukin-10 stoichiometry and the importance of deglycosylation in their crystallization.
|
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Eur J Biochem, 262,
134-141.
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K.E.Mogensen,
M.Lewerenz,
J.Reboul,
G.Lutfalla,
and
G.Uzé
(1999).
The type I interferon receptor: structure, function, and evolution of a family business.
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J Interferon Cytokine Res, 19,
1069-1098.
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P.Stordeur,
and
M.Goldman
(1998).
Interleukin-10 as a regulatory cytokine induced by cellular stress: molecular aspects.
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Int Rev Immunol, 16,
501-522.
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S.D.Spencer,
F.Di Marco,
J.Hooley,
S.Pitts-Meek,
M.Bauer,
A.M.Ryan,
B.Sordat,
V.C.Gibbs,
and
M.Aguet
(1998).
The orphan receptor CRF2-4 is an essential subunit of the interleukin 10 receptor.
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J Exp Med, 187,
571-578.
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U.Reineke,
R.Sabat,
H.D.Volk,
and
J.Schneider-Mergener
(1998).
Mapping of the interleukin-10/interleukin-10 receptor combining site.
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Protein Sci, 7,
951-960.
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R.J.Simpson,
A.Hammacher,
D.K.Smith,
J.M.Matthews,
and
L.D.Ward
(1997).
Interleukin-6: structure-function relationships.
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Protein Sci, 6,
929-955.
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A.Zdanov,
C.Schalk-Hihi,
and
A.Wlodawer
(1996).
Crystal structure of human interleukin-10 at 1.6 A resolution and a model of a complex with its soluble receptor.
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Protein Sci, 5,
1955-1962.
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PDB code:
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R.Radhakrishnan,
L.J.Walter,
A.Hruza,
P.Reichert,
P.P.Trotta,
T.L.Nagabhushan,
and
M.R.Walter
(1996).
Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray crystallography.
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Structure, 4,
1453-1463.
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PDB code:
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U.Reineke,
R.Sabat,
A.Kramer,
R.D.Stigler,
M.Seifert,
T.Michel,
H.D.Volk,
and
J.Schneider-Mergener
(1996).
Mapping protein-protein contact sites using cellulose-bound peptide scans.
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Mol Divers, 1,
141-148.
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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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