1ok9: Difference between revisions

Revision as of 09:32, 28 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:1ok9.png

Template:STRUCTURE 1ok9

DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.

Template:ABSTRACT PUBMED 14734808

About this StructureAbout this Structure

1OK9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Complement regulation at the molecular level: the structure of decay-accelerating factor., Lukacik P, Roversi P, White J, Esser D, Smith GP, Billington J, Williams PA, Rudd PM, Wormald MR, Harvey DJ, Crispin MD, Radcliffe CM, Dwek RA, Evans DJ, Morgan BP, Smith RA, Lea SM, Proc Natl Acad Sci U S A. 2004 Feb 3;101(5):1279-84. Epub 2004 Jan 20. PMID:14734808

Page seeded by OCA on Mon Jul 28 09:32:36 2008

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

OCA

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-'''DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.'''
+===DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.===
-==Overview==
+<!--
-The human complement regulator CD55 is a key molecule protecting self-cells from complement-mediated lysis. X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution. The stalk linking the four SCR domains to the glycosylphosphatidylinositol anchor is extended by the addition of 11 highly charged O-glycans and positions the domains an estimated 177 A above the membrane. Mutation mapping and hydrophobic potential analysis suggest that the interaction with the convertase, and thus complement regulation, depends on the burial of a hydrophobic patch centered on the linker between SCR domains 2 and 3.
+The line below this paragraph, {{ABSTRACT_PUBMED_14734808}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_14734808}}
 ==About this Structure==
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 [[Category: Regulator of complement]]
 [[Category: Short consensus repeat domain]]
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