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Book: Class II cytokines

Zdanov, Alexander

2007

Author's details	ed. Alexander Zdanov
Language	English
Size	211 S. : Ill., graph. Darst.
Publisher	Transworld Research Network
Publishing place	Trivandrum
Publishing country	India
Document type	Book
HBZ-ID	HT015633003
ISBN	81-7895-286-6 ; 978-81-7895-286-4
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: Structural analysis of cytokines comprising the IL-10 family.

Zdanov, Alexander

Cytokine & growth factor reviews

2010 Volume 21, Issue 5, Page(s) 325–330

Abstract: Interleukin-10 (IL-10) family of cytokines includes a number of its viral homologs and eight cellular cytokines (IL-19, IL-20, IL-22, IL-24, IL-26, IL-28A, IL-28B, and IL-29). The latter three proteins are also known as IFN-λ2, IFN-λ3, and IFN-λ1, and ... ...

Abstract	Interleukin-10 (IL-10) family of cytokines includes a number of its viral homologs and eight cellular cytokines (IL-19, IL-20, IL-22, IL-24, IL-26, IL-28A, IL-28B, and IL-29). The latter three proteins are also known as IFN-λ2, IFN-λ3, and IFN-λ1, and are recognized as type III (or λ) interferons. Most of the cellular homologs of IL-10 are monomeric in solution, whereas IL-10 and its viral homologs are intercalated dimers consisting of two helical bundle domains topologically similar to the monomeric members of the family. A classical four-helix bundle, a signature element of all helical cytokines, is always found as part of the domain of each member of the IL-10 family. The only crystal structures of these cytokine receptors that have been determined to date are for their extracellular domains (ECDs). Each ECD consists of two β-sandwich domains connected in the middle by a linkage. Signal transduction occurs when a cytokine binds to its two appropriate receptor chains. IL-10 and its viral homologs use the same IL-10 receptor system, whereas the cellular homologs of IL-10 use their own receptors, which in some cases may overlap and be used in different pairwise combinations. The known structures of binary complexes allowed for marking of the receptor binding site, which always includes helix A, loop AB and helix F (IL-10 notations) on the side of a ligand, loops of the N-terminal and C-terminal domains directed toward the ligand, and the interdomain linkage of the ECD. An analysis of the published structures of both the binary and ternary complexes of all helical cytokines allowed for the generation of a model of the signaling complex of IL-10. The receptor binding site I of the high affinity receptor IL-10R1 is exactly the same as in the crystal structure of the binary IL-10/sIL-10R1 complex, whereas the receptor binding site II is located on the surface of the first and the third helices of the four-helix bundle. The receptor/receptor interface, or site III, is formed between the C-terminal domains of IL-10R1 and IL-10R2.
MeSH term(s)	Animals ; Humans ; Interleukin-10/chemistry ; Interleukin-10/metabolism ; Interleukin-10 Receptor alpha Subunit/chemistry ; Interleukin-10 Receptor alpha Subunit/metabolism ; Interleukin-10 Receptor beta Subunit/chemistry ; Interleukin-10 Receptor beta Subunit/metabolism ; Models, Molecular ; Protein Conformation ; Signal Transduction
Chemical Substances	Interleukin-10 Receptor alpha Subunit ; Interleukin-10 Receptor beta Subunit ; Interleukin-10 (130068-27-8)
Language	English
Publishing date	2010-09-16
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	1330534-7
ISSN	1879-0305 ; 1359-6101
ISSN (online)	1879-0305
ISSN	1359-6101
DOI	10.1016/j.cytogfr.2010.08.003
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Article: Structural studies of the interleukin-19 subfamily of cytokines.

Zdanov, Alexander

Vitamins and hormones

2006 Volume 74, Page(s) 61–76

Abstract: The interleukin-19 (IL-19) subfamily of cytokines is part of a larger family of homologs of IL-10 that includes two groups of proteins: five viral cytokines, and eight cellular cytokines, having quite different biological activities. Among proteins of ... ...

Abstract	The interleukin-19 (IL-19) subfamily of cytokines is part of a larger family of homologs of IL-10 that includes two groups of proteins: five viral cytokines, and eight cellular cytokines, having quite different biological activities. Among proteins of the latter group, IL-19, IL-20, IL-22, and IL-24 were suggested to form a structurally unique IL-19 subfamily characterized by their structural features and aggregation state as monomers. IFN-lambda1, IFN-lambda2, and IFN-lambda3 are likely to belong to this subfamily, and it is still not clear whether IL-26 belongs to it or not. In spite of their differences in biological function, all cellular homologs of IL-10 used for signaling a set of five overlapping membrane-bound receptors: three long receptor chains (IL-20R1, IL-22R1, and IFN-lambdaR) and two short receptor chains (IL-20R2 and IL-10R2). Signal transduction is initiated when a cytokine binds two receptor chains, one long and one short, forming a ternary complex. Crystal structures of IL-19 and IL-22 showed that these cytokines consist of seven amphipathic helices of different length organized in helical bundle, covering an extensive hydrophobic core. Based on the similarity of the structures with the structure of a single domain of IL-10, and with the crystal structure of a binary IL-10/IL-10R1 complex, putative receptor binding sites on the surface of IL-19 and IL-22 were identified. This chapter summarizes the available structural data on the IL-19 subfamily of cytokines and their putative ligand/receptor complexes.
MeSH term(s)	Cytokines/chemistry ; Humans ; Interleukins/chemistry ; Protein Conformation ; Receptors, Interleukin/chemistry
Chemical Substances	Cytokines ; IL19 protein, human ; Interleukins ; Receptors, Interleukin
Language	English
Publishing date	2006
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	201161-x
ISSN	2162-2620 ; 0083-6729
ISSN (online)	2162-2620
ISSN	0083-6729
DOI	10.1016/S0083-6729(06)74003-1
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Article: Structural features of the interleukin-10 family of cytokines.

Zdanov, Alexander

Current pharmaceutical design

2004 Volume 10, Issue 31, Page(s) 3873–3884

Abstract: The interleukin-10 (IL-10) family of cytokines includes IL-10, a number of its viral gene homologs, and eight recently discovered cellular cytokines (IL-19, IL-20, IL-22, IL-24, IL-26, IFN-lambda1, IFN-lambda2, IFN-lambda3). IL-10 is an intercalated ... ...

Abstract	The interleukin-10 (IL-10) family of cytokines includes IL-10, a number of its viral gene homologs, and eight recently discovered cellular cytokines (IL-19, IL-20, IL-22, IL-24, IL-26, IFN-lambda1, IFN-lambda2, IFN-lambda3). IL-10 is an intercalated dimer consisting of two six-helix bundle domains. Signal transduction occurs when each domain of IL-10 binds to two receptor chains, IL-10R1 and IL-10R2. Viral homologs use the same IL-10 receptor system, while cellular homologs use their own receptors: three long receptor chains (IL-20R1, IL-22R1 and IFN-lambda1R1) and two short receptor chains (IL-20R2 and IL-10R2). Most of the cellular homologs belong to the IL-19 subfamily of cytokines including IL-19, IL-20, IL-22 and IL-24. It is likely that IFN-lambda1, IFN-lambda2, and IFN-lambda3 also belong to the same subfamily. All these proteins are monomers in solution. Crystal structures of IL-19 and IL-22 show that the molecules consist of seven helices (A-G) forming a seven-helix bundle with compact hydrophobic core inside. Structures of complexes of IL-10 and CMVIL-10 with an extracellular domain of high affinity receptor IL-10R1 (sIL-10R1) showed that ligand/receptor interactions are of mostly polar nature, with two hydrophobic patches around receptor residues Tyr43 and Phe143 at the top and bottom of the interface. The location and structure of the binding site for the second receptor chain are still unknown. It has also been shown that in the case of IL-19 and IL-20, IL-20R2 rather than IL-20R1 is a high-affinity receptor chain. This review summarizes all published three-dimensional structures of the cytokines representing the IL-10 family of homologs, including the IL-19 subfamily and their interaction with appropriate receptors.
MeSH term(s)	Cytokines/chemistry ; Cytokines/classification ; Humans ; Interleukin-10/chemistry ; Interleukin-10/classification ; Models, Molecular ; Protein Conformation
Chemical Substances	Cytokines ; Interleukin-10 (130068-27-8)
Language	English
Publishing date	2004-05-27
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ZDB-ID	1304236-1
ISSN	1873-4286 ; 1381-6128
ISSN (online)	1873-4286
ISSN	1381-6128
DOI	10.2174/1381612043382602
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Book: Class II cytokines 2007

Zdanov, Alexander

2007

Author's details	editor, Alexander Zdanov
Keywords	Cytokines.
Language	English
Size	211 p. :, ill. (chiefly col.) ;, 22 cm.
Publisher	Transworld Research Network
Publishing place	Kerala, India
Document type	Book
ISBN	9788178952864 ; 8178952866
Database	NAL-Catalogue (AGRICOLA)

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Book: Class II cytokines 2007

Zdanov, Alexander

2007

Author's details	editor, Alexander Zdanov
MeSH term(s)	Cytokines
Language	English
Size	211 p. :, ill.
Publisher	Transworld Research Network
Publishing place	Kerala, India
Document type	Book
ISBN	9788178952864 ; 8178952866
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: A new look at cytokine signaling.

Zdanov, Alexander / Wlodawer, Alexander

Cell

2008 Volume 132, Issue 2, Page(s) 179–181

Abstract: Signal transduction is initiated when a cytokine binds to the extracellular domains of its receptors, bringing them together and triggering a complicated sequence of events inside the cell. In this issue, LaPorte et al. (2008) present crystal structures ... ...

Abstract	Signal transduction is initiated when a cytokine binds to the extracellular domains of its receptors, bringing them together and triggering a complicated sequence of events inside the cell. In this issue, LaPorte et al. (2008) present crystal structures of three signaling complexes of the cytokines interleukin-4 and interleukin-13 with their receptors, showing how events taking place outside the cell may affect the specificity of signal transduction.
MeSH term(s)	Crystallization ; Cytokines/chemistry ; Cytokines/metabolism ; Dimerization ; Humans ; Interleukin-13/chemistry ; Interleukin-13/metabolism ; Interleukin-4/chemistry ; Interleukin-4/metabolism ; Ligands ; Models, Biological ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Cytokine/chemistry ; Receptors, Cytokine/metabolism ; Receptors, Interleukin-13/chemistry ; Receptors, Interleukin-13/metabolism ; Receptors, Interleukin-4/chemistry ; Receptors, Interleukin-4/metabolism ; Signal Transduction
Chemical Substances	Cytokines ; Interleukin-13 ; Ligands ; Receptors, Cytokine ; Receptors, Interleukin-13 ; Receptors, Interleukin-4 ; Interleukin-4 (207137-56-2)
Language	English
Publishing date	2008-01-25
Publishing country	United States
Document type	Comment ; Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2008.01.006
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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
Database	MEDical Literature Analysis and Retrieval System OnLINE

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