1rid

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(Replacing page with '<span style='background-color: yellow;'>For additional information see '''2009, December:''' at Retractions and Fraud.</span></br>REMOVED: The PDB entry 1rid was removed.')
 
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[[Image:1rid.gif|left|200px]]
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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.
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{{Structure
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|PDB= 1rid |SIZE=350|CAPTION= <scene name='initialview01'>1rid</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=IDS:O2-SULFO-GLUCURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>
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|ACTIVITY=
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|GENE= C3L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus])
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|DOMAIN=
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|RELATEDENTRY=[[1g40|1G40]], [[1g44|1G44]]
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1rid PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rid RCSB]</span>
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}}
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'''Vaccinia Complement Protein in Complex with Heparin'''
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==Overview==
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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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==About this Structure==
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1RID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RID OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15178763 15178763]
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[[Category: Single protein]]
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[[Category: Vaccinia virus]]
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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: regulation]]
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[[Category: scr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:28:34 2008''
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Current revision

For additional information see 2009, December: at Retractions and Fraud.</br>REMOVED: The PDB entry 1rid was removed.

Proteopedia Page Contributors and Editors (what is this?)

OCA, Eric Martz

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