1vlk
From Proteopedia
(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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| - | [[Image:1vlk.gif|left|200px]]<br /><applet load="1vlk" size=" | + | [[Image:1vlk.gif|left|200px]]<br /><applet load="1vlk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vlk, resolution 1.9Å" /> | caption="1vlk, resolution 1.9Å" /> | ||
'''STRUCTURE OF VIRAL INTERLEUKIN-10'''<br /> | '''STRUCTURE OF VIRAL INTERLEUKIN-10'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Epstein-Barr virus protein BCRF1, an analog of | + | 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== | ==About this Structure== | ||
| - | 1VLK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http:// | + | 1VLK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:36 2008'' |
Revision as of 13:36, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 15:36:36 2008
