1y6n
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(New page: 200px<br /> <applet load="1y6n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y6n, resolution 2.7Å" /> '''Crystal structure of...)
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Revision as of 18:09, 12 November 2007
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Crystal structure of Epstein-Barr virus IL-10 mutant (A87I) complexed with the soluble IL-10R1 chain
Overview
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.
About this Structure
1Y6N is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain., Yoon SI, Jones BC, Logsdon NJ, Walter MR, Structure. 2005 Apr;13(4):551-64. PMID:15837194
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