1rid
From Proteopedia
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- | [[Image:1rid.gif|left|200px]] | + | [[Image:1rid.gif|left|200px]] |
- | + | ||
- | '''Vaccinia Complement Protein in Complex with Heparin''' | + | {{Structure |
+ | |PDB= 1rid |SIZE=350|CAPTION= <scene name='initialview01'>1rid</scene>, resolution 2.1Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= C3L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus]) | ||
+ | }} | ||
+ | |||
+ | '''Vaccinia Complement Protein in Complex with Heparin''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1RID is a [ | + | 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]. |
==Reference== | ==Reference== | ||
- | 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:// | + | 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] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vaccinia virus]] | [[Category: Vaccinia virus]] | ||
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[[Category: scr]] | [[Category: scr]] | ||
- | ''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 13:52:01 2008'' |
Revision as of 11:52, 20 March 2008
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, resolution 2.1Å | |||||||
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Gene: | C3L (Vaccinia virus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Vaccinia Complement Protein in Complex with Heparin
Overview
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.
About this Structure
1RID is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.
Reference
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
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