Interleukin-10: Difference between revisions

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== '''Interleukin-10'''  ==
== '''Interleukin-10'''  ==
[[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]]''' 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 generating a conformational change that is required for IL-10R2 to be able to associate and form the ternary complex <ref name="ref1">PMID:16982608</ref>.  The affinity of IL-10R1 and Il-10R2 are not considered to 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 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.  
'''[[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"/>.  
<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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