1vlk: Difference between revisions
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<StructureSection load='1vlk' size='340' side='right'caption='[[1vlk]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1vlk' size='340' side='right'caption='[[1vlk]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vlk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1vlk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLK FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlk OCA], [https://pdbe.org/1vlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlk RCSB], [https://www.ebi.ac.uk/pdbsum/1vlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlk ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlk OCA], [https://pdbe.org/1vlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlk RCSB], [https://www.ebi.ac.uk/pdbsum/1vlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlk ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/IL10H_EBVB9 IL10H_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.<ref>PMID:2161559</ref> <ref>PMID:9310490</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human gammaherpesvirus 4]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Schalk-Hihi | [[Category: Schalk-Hihi C]] | ||
[[Category: Wlodawer | [[Category: Wlodawer A]] | ||
[[Category: Zdanov | [[Category: Zdanov A]] | ||
Revision as of 16:25, 9 May 2024
STRUCTURE OF VIRAL INTERLEUKIN-10STRUCTURE 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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