Accessibility navigation


Mapping CD55 function: the structure of two pathogen-binding domains at 1.7 A

Williams, P., Chaudhry, Y., Goodfellow, I. G., Billington, J., Powell, R., Spiller, O. B., Evans, D. J. and Lea, S. (2003) Mapping CD55 function: the structure of two pathogen-binding domains at 1.7 A. The Journal of Biological Chemistry, 278 (12). pp. 10691-6. ISSN 1083-351X

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1074/jbc.M212561200

Abstract/Summary

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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10910
Uncontrolled Keywords:Animals, Antigens, CD55/*chemistry/physiology, Bacterial Adhesion, Binding Sites, CHO Cells, Complement Activation, Crystallography, X-Ray, Hamsters, Human, Receptors, Virus/chemistry/physiology, Recombinant Proteins/chemistry, Support, Non-U.S. Gov't

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation