1vlk
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(New page: 200px<br /><applet load="1vlk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vlk, resolution 1.9Å" /> '''STRUCTURE OF VIRAL IN...)
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Revision as of 02:49, 21 November 2007
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STRUCTURE OF VIRAL INTERLEUKIN-10
Overview
The 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.
About this Structure
1VLK is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
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
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