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| [[Image:1rid.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1rid| PDB=1rid | SCENE= }} | | {{STRUCTURE_1rid| PDB=1rid | SCENE= }} |
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| '''Vaccinia Complement Protein in Complex with Heparin'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15178763}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15178763 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15178763}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Regulation]] | | [[Category: Regulation]] |
| [[Category: Scr]] | | [[Category: Scr]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:31:56 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:18:58 2008'' |
