1vlk: Difference between revisions
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[[Image:1vlk.gif|left|200px]] | [[Image:1vlk.gif|left|200px]] | ||
'''STRUCTURE OF VIRAL INTERLEUKIN-10''' | {{Structure | ||
|PDB= 1vlk |SIZE=350|CAPTION= <scene name='initialview01'>1vlk</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= | |||
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'''STRUCTURE OF VIRAL INTERLEUKIN-10''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VLK is a [ | 1VLK is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9159483 9159483] | ||
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:47:11 2008'' | ||
Revision as of 12:47, 20 March 2008
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| 1vlk, resolution 1.9Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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