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|1h2q, resolution 3.00Å ()|
|Related:||1h03, 1h04, 1h2p, 1m11, 1nwv, 1ojv, 1ojw, 1ojy, 1ok1, 1ok2, 1ok3, 1ok9, 1uot|
HUMAN CD55 DOMAINS 3 & 4
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.
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, J Biol Chem. 2003 Mar 21;278(12):10691-6. Epub 2002 Dec 22. PMID:12499389
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- 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. PMID:12499389 doi:http://dx.doi.org/10.1074/jbc.M212561200
- Lea S, Powell R, Evans D. Crystallization and preliminary X-ray diffraction analysis of a biologically active fragment of CD55. Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1198-200. PMID:10329784