1vlk: Difference between revisions
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'''STRUCTURE OF VIRAL INTERLEUKIN-10''' | '''STRUCTURE OF VIRAL INTERLEUKIN-10''' | ||
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[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: Zdanov, A.]] | [[Category: Zdanov, A.]] | ||
[[Category: | [[Category: Cytokine]] | ||
[[Category: | [[Category: Glycoprotein]] | ||
[[Category: | [[Category: Signal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:41:06 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:41, 3 May 2008
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 Page seeded by OCA on Sat May 3 12:41:06 2008
