Interleukin-10

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<StructureSection load='2h24' size='350' side='right' caption='' scene='Sandbox_165/Interleukin-10/1' pspeed='8'>
[[Image:2h24.png|right|thumb| Figure 1. IL-10 N-Terminus of helix A ]]
[[Image:2h24.png|right|thumb| Figure 1. IL-10 N-Terminus of helix A ]]
'''[[2h24|2H24]]''' is the PDB id assigned to Interleukin-10 (IL-10) after the determination of the crystal structure. IL-10 is a ternary complex that requires specific assembly for proper function. The IL-10 complex is composed of IL-10,IL-10R1,IL-10R2 (R=receptor). The initial step is the formation of IL-10 and IL-10R1, a binary complex that generates a conformational change. This conformational change is required for IL-10R2 to be able to associate with the binary complex and form the ternary complex <ref name="ref1">PMID:16982608</ref>.
'''[[2h24|2H24]]''' is the PDB id assigned to Interleukin-10 (IL-10) after the determination of the crystal structure. IL-10 is a ternary complex that requires specific assembly for proper function. The IL-10 complex is composed of IL-10,IL-10R1,IL-10R2 (R=receptor). The initial step is the formation of IL-10 and IL-10R1, a binary complex that generates a conformational change. This conformational change is required for IL-10R2 to be able to associate with the binary complex and form the ternary complex <ref name="ref1">PMID:16982608</ref>.
The affinity of IL-10R1 and Il-10R2 are not considered to be dependent on the amino acid sequence but something more complex. There are several homolog IL-10s and mimic IL-10s that are able to bind and signal through the IL-10 receptor complex causing overlaying signals with cIL-10 <ref name="ref1"/>. The completed ternary complex activates the [http://en.wikipedia.org/wiki/JAK-STAT_signaling_pathway JAK/STAT signaling pathway].[[Image:IL10.png|left|thumb|'''Figure 2. Sequential assembly of the ternary complex''' ]] The completion of the ternary complex is dependent on the conformational changes that occur in the N terminus of the helix labelled A. The conformational changes occur when the cIL-10 binds with IL-10R1. There is a positional change of about 1 angstrom at residues between Cys-12 and Leu-46. There are structural features that allow for the large conformational changes, the structural features are a Cys-12 to Cys-108 disulfide bond at the N terminus and Leu-Leu-Leu motifat the C terminus of the AB loop<ref name="ref1"/>.
The affinity of IL-10R1 and Il-10R2 are not considered to be dependent on the amino acid sequence but something more complex. There are several homolog IL-10s and mimic IL-10s that are able to bind and signal through the IL-10 receptor complex causing overlaying signals with cIL-10 <ref name="ref1"/>. The completed ternary complex activates the [http://en.wikipedia.org/wiki/JAK-STAT_signaling_pathway JAK/STAT signaling pathway].[[Image:IL10.png|left|thumb|'''Figure 2. Sequential assembly of the ternary complex''' ]] The completion of the ternary complex is dependent on the conformational changes that occur in the N terminus of the helix labelled A. The conformational changes occur when the cIL-10 binds with IL-10R1. There is a positional change of about 1 angstrom at residues between Cys-12 and Leu-46. There are structural features that allow for the large conformational changes, the structural features are a Cys-12 to Cys-108 disulfide bond at the N terminus and Leu-Leu-Leu motifat the C terminus of the AB loop<ref name="ref1"/>.
<scene name='Sandbox_165/2h24_backbone/1'>2h24 ball and stick</scene>
<scene name='Sandbox_165/2h24_backbone/1'>2h24 ball and stick</scene>
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=='''IL-10'''==
=='''IL-10'''==
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There are many [http://en.wikipedia.org/wiki/interleukin interleukins] that fall within the cytokine class such as IL-1,IL-2,IL-3,IL-4...IL-31,IL-32,IL-33,IL-3 and IL-35.
There are many [http://en.wikipedia.org/wiki/interleukin interleukins] that fall within the cytokine class such as IL-1,IL-2,IL-3,IL-4...IL-31,IL-32,IL-33,IL-3 and IL-35.
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{{STRUCTURE_2h24| PDB=2h24| SCENE=Sandbox_165/Interleukin-10/1}}
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=Interleukin-10 and Rheumatoid Arthritis=
=Interleukin-10 and Rheumatoid Arthritis=
[[Image:Illu_synovial_joint.jpg|left|thumb|'''Figure 3. Synovial Joint''' ]]<ref>http://en.wikipedia.org/wiki/Synovial_membrane</ref>
[[Image:Illu_synovial_joint.jpg|left|thumb|'''Figure 3. Synovial Joint''' ]]<ref>http://en.wikipedia.org/wiki/Synovial_membrane</ref>
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</StructureSection>
==3D structures of interleukin==
==3D structures of interleukin==

Current revision

PDB ID 2h24

Drag the structure with the mouse to rotate

3D structures of interleukin

Interleukin


References

  1. ↑ 1.0 1.1 1.2 1.3 Yoon SI, Logsdon NJ, Sheikh F, Donnelly RP, Walter MR. Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex. J Biol Chem. 2006 Nov 17;281(46):35088-96. Epub 2006 Sep 18. PMID:16982608 doi:10.1074/jbc.M606791200
  2. ↑ Hudson LL, Rocca KM, Kuwana M, Pandey JP. Interleukin-10 genotypes are associated with systemic sclerosis and influence disease-associated autoimmune responses. Genes Immun. 2005 May;6(3):274-8. PMID:15772682
  3. ↑ Shih CM, Lee YL, Chiou HL, Hsu WF, Chen WE, Chou MC, Lin LY. The involvement of genetic polymorphism of IL-10 promoter in non-small cell lung cancer. Lung Cancer. 2005 Dec;50(3):291-7. Epub 2005 Aug 24. PMID:16122836 doi:10.1016/j.lungcan.2005.07.007
  4. ↑ 4.0 4.1 4.2 Katsikis PD, Chu CQ, Brennan FM, Maini RN, Feldmann M. Immunoregulatory role of interleukin 10 in rheumatoid arthritis. J Exp Med. 1994 May 1;179(5):1517-27. PMID:8163935
  5. ↑ http://en.wikipedia.org/wiki/Synovial_membrane
  6. ↑ 6.0 6.1 Nemec P, Goldbergova MP, Gatterova J, Vasku A, Soucek M. Association of polymorphisms in interleukin-10 gene promoter with autoantibody production in patients with rheumatoid arthritis. Ann N Y Acad Sci. 2009 Sep;1173:501-8. PMID:19758192 doi:10.1111/j.1749-6632.2009.04625.x
  7. ↑ de Waal Malefyt R, Abrams J, Bennett B, Figdor CG, de Vries JE. Interleukin 10(IL-10) inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL-10 produced by monocytes. J Exp Med. 1991 Nov 1;174(5):1209-20. PMID:1940799
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