1y6n
From Proteopedia
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, resolution 2.7Å | |||||||
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Gene: | BCRF1 (Human herpesvirus 4), IL10RA, IL10R (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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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