Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A.
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Williams P, Chaudhry Y, Goodfellow IG, Billington J, Powell R, Spiller OB, Evans DJ, Lea S
Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A.
J Biol Chem. 2003 Mar 21;278(12):10691-6. Epub 2002 Dec 22.
- PubMed ID
- 12499389 [ View in PubMed]
- 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.