1y6n: Difference between revisions

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[[Image:1y6n.gif|left|200px]]
{{Seed}}
[[Image:1y6n.png|left|200px]]


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{{STRUCTURE_1y6n|  PDB=1y6n  |  SCENE=  }}  
{{STRUCTURE_1y6n|  PDB=1y6n  |  SCENE=  }}  


'''Crystal structure of Epstein-Barr virus IL-10 mutant (A87I) complexed with the soluble IL-10R1 chain'''
===Crystal structure of Epstein-Barr virus IL-10 mutant (A87I) complexed with the soluble IL-10R1 chain===




==Overview==
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Human IL-10 (hIL-10) is a cytokine that modulates diverse immune responses. The Epstein-Barr virus (EBV) genome contains an IL-10 homolog (vIL-10) that shares high sequence and structural similarity with hIL-10. Although vIL-10 suppresses inflammatory responses like hIL-10, it cannot activate many other immunostimulatory functions performed by the cellular cytokine. These functional differences have been correlated with the approximately 1000-fold lower affinity of vIL-10, compared to hIL-10, for the IL-10R1 receptor chain. To define the structural basis for these observations, crystal structures of vIL-10 and a vIL-10 point mutant were determined bound to the soluble IL-10R1 receptor fragment (sIL-10R1) at 2.8 and 2.7 A resolution, respectively. The structures reveal that subtle changes in the conformation and dynamics of the vIL-10 AB and CD loops and an orientation change of vIL-10 on sIL-10R1 are the main factors responsible for vIL-10's reduced affinity for sIL-10R1 and its distinct biological profile.
The line below this paragraph, {{ABSTRACT_PUBMED_15837194}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15837194 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15837194}}


==About this Structure==
==About this Structure==
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[[Category: Helix bundle]]
[[Category: Helix bundle]]
[[Category: Receptor complex]]
[[Category: Receptor complex]]
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