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4og9
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/IL12B_HUMAN IL12B_HUMAN]] Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC.<ref>PMID:11114383</ref> Associates with IL23A to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.<ref>PMID:11114383</ref> [[http://www.uniprot.org/uniprot/IL23A_HUMAN IL23A_HUMAN]] Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.<ref>PMID:11114383</ref> <ref>PMID:12023369</ref> <ref>PMID:16424222</ref> | [[http://www.uniprot.org/uniprot/IL12B_HUMAN IL12B_HUMAN]] Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC.<ref>PMID:11114383</ref> Associates with IL23A to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.<ref>PMID:11114383</ref> [[http://www.uniprot.org/uniprot/IL23A_HUMAN IL23A_HUMAN]] Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.<ref>PMID:11114383</ref> <ref>PMID:12023369</ref> <ref>PMID:16424222</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein scaffolds can provide a promising alternative to antibodies for various biomedical and biotechnological applications, including therapeutics. Here we describe the design and development of the Alphabody, a protein scaffold featuring a single-chain antiparallel triple-helix coiled-coil fold. We report affinity-matured Alphabodies with favourable physicochemical properties that can specifically neutralize human interleukin (IL)-23, a pivotal therapeutic target in autoimmune inflammatory diseases such as psoriasis and multiple sclerosis. The crystal structure of human IL-23 in complex with an affinity-matured Alphabody reveals how the variable interhelical groove of the scaffold uniquely targets a large epitope on the p19 subunit of IL-23 to harness fully the hydrophobic and hydrogen-bonding potential of tryptophan and tyrosine residues contributed by p19 and the Alphabody, respectively. Thus, Alphabodies are suitable for targeting protein-protein interfaces of therapeutic importance and can be tailored to interrogate desired design and binding-mode principles via efficient selection and affinity-maturation strategies. | ||
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| + | Structural basis of IL-23 antagonism by an Alphabody protein scaffold.,Desmet J, Verstraete K, Bloch Y, Lorent E, Wen Y, Devreese B, Vandenbroucke K, Loverix S, Hettmann T, Deroo S, Somers K, Henderikx P, Lasters I, Savvides SN Nat Commun. 2014 Oct 30;5:5237. doi: 10.1038/ncomms6237. PMID:25354530<ref>PMID:25354530</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bloch, Y | + | [[Category: Bloch, Y]] |
| - | [[Category: Deroo, S | + | [[Category: Deroo, S]] |
| - | [[Category: Desmet, J | + | [[Category: Desmet, J]] |
| - | [[Category: Devreese, B | + | [[Category: Devreese, B]] |
| - | [[Category: Hendrikx, P | + | [[Category: Hendrikx, P]] |
| - | [[Category: Hettmann, T | + | [[Category: Hettmann, T]] |
| - | [[Category: Lasters, I | + | [[Category: Lasters, I]] |
| - | [[Category: Lorent, E | + | [[Category: Lorent, E]] |
| - | [[Category: Loverix, S | + | [[Category: Loverix, S]] |
| - | [[Category: Savvides, S N | + | [[Category: Savvides, S N]] |
| - | [[Category: Somers, K | + | [[Category: Somers, K]] |
| - | [[Category: Vandenbroucke, K | + | [[Category: Vandenbroucke, K]] |
| - | [[Category: Verstraete, K | + | [[Category: Verstraete, K]] |
| - | [[Category: Wen, Y | + | [[Category: Wen, Y]] |
[[Category: 4-alpha helical bundle]] | [[Category: 4-alpha helical bundle]] | ||
[[Category: Alkylation]] | [[Category: Alkylation]] | ||
Revision as of 07:43, 12 November 2014
Cytokine complex crystal form 2
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Categories: Bloch, Y | Deroo, S | Desmet, J | Devreese, B | Hendrikx, P | Hettmann, T | Lasters, I | Lorent, E | Loverix, S | Savvides, S N | Somers, K | Vandenbroucke, K | Verstraete, K | Wen, Y | 4-alpha helical bundle | Alkylation | Antagonist | Cytokine-antagonist complex | Immunoglobulin-like | N-linked glycosylation | Single-chain antiparallel triple-helix coiled-coil
