1g40: Difference between revisions

Revision as of 04:22, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1g40.png

Template:STRUCTURE 1g40

CRYSTAL STRUCTURE OF A COMPLEMENT PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANSCRYSTAL STRUCTURE OF A COMPLEMENT PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS

Template:ABSTRACT PUBMED 11207370

About this StructureAbout this Structure

1G40 is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans., Murthy KH, Smith SA, Ganesh VK, Judge KW, Mullin N, Barlow PN, Ogata CM, Kotwal GJ, Cell. 2001 Jan 26;104(2):301-11. PMID:11207370

Page seeded by OCA on Tue Jul 1 04:22:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Eric Martz

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-'''CRYSTAL STRUCTURE OF A COMPLEMENT PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS'''
+===CRYSTAL STRUCTURE OF A COMPLEMENT PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS===
-==Overview==
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-Vaccinia virus complement control protein (VCP) inhibits both pathways of complement activation through binding the third and fourth components. A homolog of mammalian regulators of complement activation, its ability to bind heparin endows VCP with additional activities of significance to viral infectivity. The structure of VCP reveals a highly extended molecule with a putative heparin recognition site at its C-terminal end. A second cluster of positive charges provides a possibly overlapping binding site for both heparin and complement components. Experiments suggested by the structure indicate that VCP can bind heparin and control complement simultaneously. This, the structure of any intact regulator of complement activation, along with attendant functional insights, will stimulate the design of new therapeutic inhibitors of complement.
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