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Article ; Online: A model of the ternary complex of interleukin-10 with its soluble receptors

Wlodawer Alexander / Magracheva Eugenia / Pletnev Sergei / Zdanov Alexander

BMC Structural Biology, Vol 5, Iss 1, p

2005 Volume 10

Abstract: Abstract Background Interleukin-10 (IL-10) is a cytokine whose main biological function is to suppress the immune response by induction of a signal(s) leading to inhibition of synthesis of a number of cytokines and their cellular receptors. Signal ... ...

Abstract	Abstract Background Interleukin-10 (IL-10) is a cytokine whose main biological function is to suppress the immune response by induction of a signal(s) leading to inhibition of synthesis of a number of cytokines and their cellular receptors. Signal transduction is initiated upon formation of a ternary complex of IL-10 with two of its receptor chains, IL-10R1 and IL-10R2, expressed on the cell membrane. The affinity of IL-10R1 toward IL-10 is very high, which allowed determination of the crystal structure of IL-10 complexed with the extracellular/soluble domain of IL-10R1, while the affinity of IL-10R2 toward either IL-10 or IL-10/sIL-10R1 complex is quite low. This so far has prevented any attempts to obtain structural information about the ternary complex of IL-10 with its receptor chains. Results Structures of the second soluble receptor chain of interleukin-10 (sIL-10R2) and the ternary complex of IL-10/sIL-10R1/sIL-10R2 have been generated by homology modeling, which allowed us to identify residues involved in ligand-receptor and receptor-receptor interactions. Conclusion The previously experimentally determined structure of the intermediate/binary complex IL-10/sIL-10R1 is the same in the ternary complex. There are two binding sites for the second receptor chain on the surface of the IL-10/sIL-10R1 complex, involving both IL-10 and sIL-10R1. Most of the interactions are hydrophilic in nature, although each interface includes two internal hydrophobic clusters. The distance between C-termini of the receptor chains is 25 Å, which is common for known structures of ternary complexes of other cytokines. The structure is likely to represent the biologically active signaling complex of IL-10 with its receptor on the surface of the cell membrane.
Keywords	Biology (General) ; QH301-705.5
Subject code	612
Language	English
Publishing date	2005-06-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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Article ; Online: A model of the ternary complex of interleukin-10 with its soluble receptors.

Pletnev, Sergei / Magracheva, Eugenia / Wlodawer, Alexander / Zdanov, Alexander

BMC structural biology

2005 Volume 5, Page(s) 10

Abstract: Background: Interleukin-10 (IL-10) is a cytokine whose main biological function is to suppress the immune response by induction of a signal(s) leading to inhibition of synthesis of a number of cytokines and their cellular receptors. Signal transduction ... ...

Abstract	Background: Interleukin-10 (IL-10) is a cytokine whose main biological function is to suppress the immune response by induction of a signal(s) leading to inhibition of synthesis of a number of cytokines and their cellular receptors. Signal transduction is initiated upon formation of a ternary complex of IL-10 with two of its receptor chains, IL-10R1 and IL-10R2, expressed on the cell membrane. The affinity of IL-10R1 toward IL-10 is very high, which allowed determination of the crystal structure of IL-10 complexed with the extracellular/soluble domain of IL-10R1, while the affinity of IL-10R2 toward either IL-10 or IL-10/sIL-10R1 complex is quite low. This so far has prevented any attempts to obtain structural information about the ternary complex of IL-10 with its receptor chains. Results: Structures of the second soluble receptor chain of interleukin-10 (sIL-10R2) and the ternary complex of IL-10/sIL-10R1/sIL-10R2 have been generated by homology modeling, which allowed us to identify residues involved in ligand-receptor and receptor-receptor interactions. Conclusion: The previously experimentally determined structure of the intermediate/binary complex IL-10/sIL-10R1 is the same in the ternary complex. There are two binding sites for the second receptor chain on the surface of the IL-10/sIL-10R1 complex, involving both IL-10 and sIL-10R1. Most of the interactions are hydrophilic in nature, although each interface includes two internal hydrophobic clusters. The distance between C-termini of the receptor chains is 25 A, which is common for known structures of ternary complexes of other cytokines. The structure is likely to represent the biologically active signaling complex of IL-10 with its receptor on the surface of the cell membrane.
MeSH term(s)	Amino Acid Sequence ; Binding Sites ; Cell Line, Tumor ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Gene Deletion ; Glycosylation ; Humans ; Hydrogen Bonding ; Interleukin-10/chemistry ; Ligands ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Interferon/chemistry ; Receptors, Interleukin/chemistry ; Receptors, Interleukin-10 ; Sequence Homology, Amino Acid ; Signal Transduction
Chemical Substances	Ligands ; Peptides ; Receptors, Interferon ; Receptors, Interleukin ; Receptors, Interleukin-10 ; Interleukin-10 (130068-27-8)
Language	English
Publishing date	2005-06-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2050440-8
ISSN	1472-6807 ; 1472-6807
ISSN (online)	1472-6807
ISSN	1472-6807
DOI	10.1186/1472-6807-5-10
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Article ; Online: Crystal structure of human interferon-λ1 in complex with its high-affinity receptor interferon-λR1.

Miknis, Zachary J / Magracheva, Eugenia / Li, Wei / Zdanov, Alexander / Kotenko, Sergei V / Wlodawer, Alexander

Journal of molecular biology

2010 Volume 404, Issue 4, Page(s) 650–664

Abstract: Interferon (IFN)-λ1 [also known as interleukin (IL)-29] belongs to the recently discovered group of type III IFNs. All type III IFNs initiate signaling processes through formation of specific heterodimeric receptor complexes consisting of IFN-λR1 and IL- ... ...

Abstract	Interferon (IFN)-λ1 [also known as interleukin (IL)-29] belongs to the recently discovered group of type III IFNs. All type III IFNs initiate signaling processes through formation of specific heterodimeric receptor complexes consisting of IFN-λR1 and IL-10R2. We have determined the structure of human IFN-λ1 complexed with human IFN-λR1, a receptor unique to type III IFNs. The overall structure of IFN-λ1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines. IFN-λR1 consists of two distinct domains having fibronectin type III topology. The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1. Composition and architecture of the interface that includes only a few direct hydrogen bonds support an idea that long-range ionic interactions between ligand and receptor govern the process of initial recognition of the molecules while hydrophobic interactions finalize it.
MeSH term(s)	Amino Acid Sequence ; Crystallography, X-Ray ; Humans ; Interferons ; Interleukins/chemistry ; Interleukins/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Structure, Quaternary ; Receptors, Interferon/chemistry ; Receptors, Interferon/metabolism ; Sequence Alignment
Chemical Substances	interferon-lambda, human ; Interleukins ; Receptors, Interferon ; Interferons (9008-11-1)
Keywords	covid19
Language	English
Publishing date	2010-10-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2010.09.068
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Article ; Online: Purification, crystallization and preliminary crystallographic studies of the complex of interferon-lambda1 with its receptor.

Magracheva, Eugenia / Pletnev, Sergei / Kotenko, Sergei / Li, Wei / Wlodawer, Alexander / Zdanov, Alexander

Acta crystallographica. Section F, Structural biology and crystallization communications

2009 Volume 66, Issue Pt 1, Page(s) 61–63

Abstract: Human interferon-lambda1 (IFN-lambda1(Ins)) and the extracellular domain of interferon-lambda1 receptor (IFN-lambda1R1) were expressed in Drosophila S2 cells and purified to homogeneity. Both IFN-lambda1(Ins) and interferon-lambda1 produced from ... ...

Abstract	Human interferon-lambda1 (IFN-lambda1(Ins)) and the extracellular domain of interferon-lambda1 receptor (IFN-lambda1R1) were expressed in Drosophila S2 cells and purified to homogeneity. Both IFN-lambda1(Ins) and interferon-lambda1 produced from Escherichia coli (IFN-lambda1(Bac)) were coupled with IFN-lambda1R1 at room temperature and the complexes were purified by gel filtration. Both complexes were crystallized; the crystals were flash-frozen at 100 K and diffraction data were collected to 2.16 and 2.1 A, respectively. Although the IFN-lambda1(Bac)-IFN-lambda1R1 and IFN-lambda1(Ins)-IFN-lambda1R1 complexes differed only in the nature of the expression system used for the ligand, their crystallization conditions and crystal forms were quite different. A search for heavy-atom derivatives as well as molecular-replacement trials are in progress.
MeSH term(s)	Animals ; Crystallization ; Crystallography, X-Ray ; Drosophila ; Humans ; Interferons ; Interleukins/chemistry ; Receptors, Interferon/chemistry
Chemical Substances	interferon-lambda, human ; Interleukins ; Receptors, Interferon ; Interferons (9008-11-1)
Language	English
Publishing date	2009-12-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	1744-3091
ISSN (online)	1744-3091
DOI	10.1107/S1744309109048817
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Article ; Online: Structure of the lamin A/C R482W mutant responsible for dominant familial partial lipodystrophy (FPLD).

Magracheva, Eugenia / Kozlov, Serguei / Stewart, Colin L / Wlodawer, Alexander / Zdanov, Alexander

Acta crystallographica. Section F, Structural biology and crystallization communications

2009 Volume 65, Issue Pt 7, Page(s) 665–670

Abstract: Proteins of the A-type lamin family, which consists of two members, lamin A and lamin C, are the major components of a thin proteinaceous filamentous meshwork, the lamina, that underlies the inner nuclear membrane. A-type lamins have recently become the ... ...

Abstract	Proteins of the A-type lamin family, which consists of two members, lamin A and lamin C, are the major components of a thin proteinaceous filamentous meshwork, the lamina, that underlies the inner nuclear membrane. A-type lamins have recently become the focus of extensive functional studies as a consequence of the linking of at least eight congenital diseases to mutations in the lamin A/C gene (LMNA). This spectrum of pathologies, which mostly manifest themselves as dominant traits, includes muscle dystrophies, dilated cardiomyopathies, the premature aging syndrome Hutchinson-Guilford progeria and familial partial lipodystrophy (FPLD). The crystal structure of the lamin A/C mutant R482W, a variant that causes FPLD, has been determined at 1.5 A resolution. A completely novel aggregation state of the C-terminal globular domain and the position of the mutated amino-acid residue suggest means by which the mutation may affect lamin A/C-protein and protein-DNA interactions.
MeSH term(s)	Allosteric Regulation ; Amino Acid Substitution/genetics ; Crystallography, X-Ray ; DNA/metabolism ; Genes, Dominant ; Humans ; Lamin Type A/chemistry ; Lamin Type A/genetics ; Lipodystrophy, Familial Partial/genetics ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Mutation/genetics ; Protein Binding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Static Electricity
Chemical Substances	Lamin Type A ; Mutant Proteins ; lamin C ; DNA (9007-49-2)
Language	English
Publishing date	2009-06-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
ISSN	1744-3091
ISSN (online)	1744-3091
DOI	10.1107/S1744309109020302
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Article ; Online: Structure and mechanism of the saposin-like domain of a plant aspartic protease.

Bryksa, Brian C / Bhaumik, Prasenjit / Magracheva, Eugenia / De Moura, Dref C / Kurylowicz, Martin / Zdanov, Alexander / Dutcher, John R / Wlodawer, Alexander / Yada, Rickey Y

The Journal of biological chemistry

2011 Volume 286, Issue 32, Page(s) 28265–28275

Abstract: Many plant aspartic proteases contain an additional sequence of ~100 amino acids termed the plant-specific insert, which is involved in host defense and vacuolar targeting. Similar to all saposin-like proteins, the plant-specific insert functions via ... ...

Abstract	Many plant aspartic proteases contain an additional sequence of ~100 amino acids termed the plant-specific insert, which is involved in host defense and vacuolar targeting. Similar to all saposin-like proteins, the plant-specific insert functions via protein-membrane interactions; however, the structural basis for such interactions has not been studied, and the nature of plant-specific insert-mediated membrane disruption has not been characterized. In the present study, the crystal structure of the saposin-like domain of potato aspartic protease was resolved at a resolution of 1.9 Å, revealing an open V-shaped configuration similar to the open structure of human saposin C. Notably, vesicle disruption activity followed Michaelis-Menten-like kinetics, a finding not previously reported for saposin-like proteins including plant-specific inserts. Circular dichroism data suggested that secondary structure was pH-dependent in a fashion similar to influenza A hemagglutinin fusion peptide. Membrane effects characterized by atomic force microscopy and light scattering indicated bilayer solubilization as well as fusogenic activity. Taken together, the present study is the first report to elucidate the membrane interaction mechanism of plant saposin-like domains whereby pH-dependent membrane interactions resulted in bilayer fusogenic activity that probably arose from a viral type pH-dependent helix-kink-helix motif at the plant-specific insert N terminus.
MeSH term(s)	Aspartic Acid Proteases/chemistry ; Helix-Turn-Helix Motifs ; Humans ; Plant Proteins/chemistry ; Protein Structure, Tertiary ; Saposins/chemistry ; Solanum tuberosum/enzymology ; Structural Homology, Protein ; Structure-Activity Relationship
Chemical Substances	Plant Proteins ; Saposins ; Aspartic Acid Proteases (EC 3.4.-)
Language	English
Publishing date	2011-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.252619
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Article: Characterization of the recombinant extracellular domains of human interleukin-20 receptors and their complexes with interleukin-19 and interleukin-20.

Pletnev, Sergei / Magracheva, Eugenia / Kozlov, Serguei / Tobin, Gregory / Kotenko, Sergei V / Wlodawer, Alexander / Zdanov, Alexander

Biochemistry

2003 Volume 42, Issue 43, Page(s) 12617–12624

Abstract: The soluble extracellular domains of human interleukin-20 (IL-20) receptors I and II (sIL-20R1 and sIL20R2), along with their ligands IL-19 and IL-20, were expressed in Drosophila S2 cells and purified to homogeneity. Formation of the receptor/receptor ... ...

Abstract	The soluble extracellular domains of human interleukin-20 (IL-20) receptors I and II (sIL-20R1 and sIL20R2), along with their ligands IL-19 and IL-20, were expressed in Drosophila S2 cells and purified to homogeneity. Formation of the receptor/receptor and ligand/receptor complexes was studied by size exclusion chromatography. Both ligands and soluble receptors were found to be monomeric in solution; homo- or heterodimers are not formed even at elevated concentrations. Under native conditions, both IL-19 and IL-20 form stable ternary 1:1:1 complexes with the sIL-20R1 and sIL20R2 receptors, as well as high-affinity binary complexes with sIL-20R2. Unexpectedly, sIL-20R1 does not bind on its own to either IL-19 or IL-20. Thus, one of the possible consecutive mechanisms of formation of the signaling ternary complex may involve two steps: first, the ligand binds to receptor II, creating a high-affinity binding site for the receptor I, and only then does receptor I complete the complex.
MeSH term(s)	Chromatography, Gel ; Electrophoresis, Polyacrylamide Gel ; Glycosylation ; Humans ; Interleukin-10/isolation & purification ; Interleukin-10/metabolism ; Interleukins/isolation & purification ; Interleukins/metabolism ; Receptors, Interleukin/chemistry ; Receptors, Interleukin/isolation & purification ; Receptors, Interleukin/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism
Chemical Substances	IL19 protein, human ; Interleukins ; Receptors, Interleukin ; Recombinant Proteins ; Interleukin-10 (130068-27-8) ; interleukin 20 (U91R7IMG8U)
Language	English
Publishing date	2003-10-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi0354583
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Article: Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.

Chang, Changsoo / Magracheva, Eugenia / Kozlov, Serguei / Fong, Steven / Tobin, Gregory / Kotenko, Sergei / Wlodawer, Alexander / Zdanov, Alexander

The Journal of biological chemistry

2002 Volume 278, Issue 5, Page(s) 3308–3313

Abstract: Interleukin-19 (IL-19) is a novel cytokine that was initially identified during a sequence data base search aimed at finding potential IL-10 homologs. IL-19 shares a receptor complex with IL-20, indicating that the biological activities of these two ... ...

Abstract	Interleukin-19 (IL-19) is a novel cytokine that was initially identified during a sequence data base search aimed at finding potential IL-10 homologs. IL-19 shares a receptor complex with IL-20, indicating that the biological activities of these two cytokines overlap and that both may play an important role in regulating development and proper functioning of the skin. We determined the crystal structure of human recombinant IL-19 and refined it at 1.95-A resolution to an R-factor of 0.157. Unlike IL-10, which forms an intercalated dimer, the molecule of IL-19 is a monomer made of seven amphipathic helices, A-G, creating a unique helical bundle. On the basis of the observed structure, we propose that IL-19, IL-20, and other putative members of the proposed IL-10 family together form a distinct subfamily of helical cytokines.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Line ; Conserved Sequence ; Crystallography, X-Ray ; Drosophila melanogaster ; Humans ; Interleukin-10/chemistry ; Interleukins/chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Sensitivity and Specificity ; Sequence Alignment ; Transfection
Chemical Substances	IL19 protein, human ; Interleukins ; Recombinant Proteins ; Interleukin-10 (130068-27-8) ; interleukin 20 (U91R7IMG8U)
Language	English
Publishing date	2002-10-25
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M208602200
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