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| - | | + | <span style='background-color: yellow;'>For additional information see '''2009, December:''' at [[Retractions and Fraud]].</span></br>REMOVED: The PDB entry 1rid was removed. |
| - | ==Vaccinia Complement Protein in Complex with Heparin==
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| - | <StructureSection load='1rid' size='340' side='right' caption='[[1rid]], [[Resolution|resolution]] 2.10Å' scene=''> | + | |
| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[1rid]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccw Vaccw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RID FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g40|1g40]], [[1g44|1g44]]</td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C3L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 VACCW])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rid OCA], [http://pdbe.org/1rid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rid RCSB], [http://www.ebi.ac.uk/pdbsum/1rid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rid ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/VCP_VACCW VCP_VACCW]] Serves to protect the virus against complement attack by inhibiting both classical and alternative pathways of complement activation. Binds C3b and C4b.<ref>PMID:1731333</ref> <ref>PMID:18287241</ref>
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| - | == Evolutionary Conservation ==
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| - | [[Image:Consurf_key_small.gif|200px|right]]
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| - | Check<jmol>
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| - | <jmolCheckbox>
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| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/1rid_consurf.spt"</scriptWhenChecked>
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| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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| - | <text>to colour the structure by Evolutionary Conservation</text>
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| - | </jmolCheckbox>
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| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rid ConSurf].
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| - | <div style="clear:both"></div>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Vaccinia virus complement control protein (VCP), a homolog of the regulators of the complement activation family of proteins, inhibits complement activation through mechanisms similar to human fluid-phase complement regulators factor H and C4b-binding protein. VCP has a heparin-binding activity that assists vaccinia in host interactions. Interaction with cell-surface polyanions like heparin is centrally important in the functioning of fluid-phase complement regulators and is the basis of host-target discrimination by the alternative pathway. We report the structure of VCP in complex with a heparin decasaccharide, which reveals changes in VCP that might be pertinent to complement regulation. Properties that VCP shares with fluid-phase complement regulators suggest that such conformational changes may be of relevance in the functioning of other complement regulators. Additionally, comparison of VCP-heparin interactions with potentially similar interactions in factor H might enable understanding of the structural basis of familial hemolytic uremic syndrome, attributed to mutational disruption of heparin and C3b binding by factor H.
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| - | Structure of vaccinia complement protein in complex with heparin and potential implications for complement regulation.,Ganesh VK, Smith SA, Kotwal GJ, Murthy KH Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8924-9. Epub 2004 Jun 3. PMID:15178763<ref>PMID:15178763</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 1rid" style="background-color:#fffaf0;"></div>
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| - | ==See Also==
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| - | *[[Retractions and Fraud|Retractions and Fraud]]
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| - | *[[User:Eric Martz/Entertaining PDB codes|User:Eric Martz/Entertaining PDB codes]]
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Vaccw]]
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| - | [[Category: Ganesh, V K]]
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| - | [[Category: Kotwal, G J]]
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| - | [[Category: Murthy, K H.M]]
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| - | [[Category: Smith, S A]]
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| - | [[Category: Complement]]
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| - | [[Category: Immune system]]
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| - | [[Category: Regulation]]
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| - | [[Category: Scr]]
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