1H03
Human CD55 domains 3 & 4
Summary for 1H03
Entry DOI | 10.2210/pdb1h03/pdb |
Related | 1H04 1H2P 1H2Q 1M11 |
Descriptor | COMPLEMENT DECAY-ACCELERATING FACTOR (2 entities in total) |
Functional Keywords | immune system protein, complement decay accelerating factor, enteroviral receptor, bacterial receptor, ligand for cd97, complement pathway, alternative splicing, gpi-anchor |
Biological source | HOMO SAPIENS (HUMAN) |
Total number of polymer chains | 2 |
Total formula weight | 27172.10 |
Authors | Williams, P.,Chaudhry, Y.,Goodfellow, I.,Billington, J.,Spiller, B.,Evans, D.J.,Lea, S.M. (deposition date: 2002-06-11, release date: 2003-03-20, Last modification date: 2024-11-20) |
Primary citation | Williams, P.,Chaudhry, Y.,Goodfellow, I.,Billington, J.,Powell, R.,Spiller, O.,Evans, D.J.,Lea, S.M. Mapping Cd55 Function. The Structure of Two Pathogen-Binding Domains at 1.7 A J.Biol.Chem., 278:10691-, 2003 Cited by 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. PubMed: 12499389DOI: 10.1074/JBC.M212561200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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