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1H03

Human CD55 domains 3 & 4

Summary for 1H03
Entry DOI10.2210/pdb1h03/pdb
Related1H04 1H2P 1H2Q 1M11
DescriptorCOMPLEMENT DECAY-ACCELERATING FACTOR (2 entities in total)
Functional Keywordsimmune system protein, complement decay accelerating factor, enteroviral receptor, bacterial receptor, ligand for cd97, complement pathway, alternative splicing, gpi-anchor
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains2
Total formula weight27172.10
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 citationWilliams, 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: 12499389
DOI: 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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