1vlk
STRUCTURE OF VIRAL INTERLEUKIN-10
Structural highlights
FunctionIL10H_EBVB9 Plays a role in masking infected cells for immune recognition by cytotoxic T-lymphocytes. Down-regulates the expression of the host TAP1 gene (transporter associated with antigen processing), thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules. Inhibits IFN-gamma synthesis.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of Epstein-Barr virus protein BCRF1, an analog of cellular interleukin-10 (IL-10), has been determined at the resolution of 1.9 A and refined to an R-factor 0.191. The structure of this cytokine is similar to that of human IL-10 (hIL-10), forming an intercalated dimer of two 17 kDa polypeptides related by a crystallographic 2-fold symmetry axis. BCRF1 exhibits novel conformations of the N-terminal coil and of the loop between helices A and B compared to hIL-10. These regions are likely to be involved in binding of one or more components of the IL-10 receptor system, and thus the structural differences may account for the lower binding affinity and limited spectrum of biological activities of viral IL-10, compared to hIL-10. Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10.,Zdanov A, Schalk-Hihi C, Menon S, Moore KW, Wlodawer A J Mol Biol. 1997 May 2;268(2):460-7. PMID:9159483[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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