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	J. Biol. Chem. Mar (2003); 278(12):10691-6
Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A.
Williams P, Chaudhry Y, Goodfellow IG, Billington J, Powell R, Spiller OB, Evans DJ, Lea S
Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, United Kingdom.
Abstract: Decay-accelerating factor (CD55), a regulator of the alternative and classical pathways of complement activation, is expressed on all serum-exposed cells. It is used by pathogens, including many enteroviruses and uropathogenic Escherichia coli, as a receptor prior to infection. We describe the x-ray structure of a pathogen-binding fragment of human CD55 at 1.7 A resolution containing two of the three domains required for regulation of human complement. We have used mutagenesis to map biological functions onto the molecule; decay-accelerating activity maps to a single face of the molecule, whereas bacterial and viral pathogens recognize a variety of different sites on CD55.
[PUBMED: 12499389]