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1OK2

Decay accelerating factor (CD55): the structure of an intact human complement regulator.

Summary for 1OK2
Entry DOI10.2210/pdb1ok2/pdb
Related1H03 1H04 1H2P 1H2Q 1M11 1NWV 1OJV 1OJW 1OJY 1OK1 1OK3 1OK9 1UOT 1UPN
DescriptorCOMPLEMENT DECAY-ACCELERATING FACTOR, ACETATE ION, SULFATE ION, ... (5 entities in total)
Functional Keywordsregulator of complement pathway, regulator of complement, decay acceleration of c3/c5 convertases, pathogen receptor, short consensus repeat domains
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains2
Total formula weight57606.48
Authors
Primary citationLukacik, P.,Roversi, P.,White, J.,Esser, D.,Smith, G.P.,Billington, J.,Williams, P.A.,Rudd, P.M.,Wormald, M.R.,Harvey, D.J.,Crispin, M.D.M.,Radcliffe, C.M.,Dwek, R.A.,Evans, D.J.,Morgan, B.P.,Smith, R.A.G.,Lea, S.M.
Complement Regulation at the Molecular Level: The Structure of Decay-Accelerating Factor
Proc.Natl.Acad.Sci.USA, 101:1279-, 2004
Cited by
PubMed Abstract: The human complement regulator CD55 is a key molecule protecting self-cells from complement-mediated lysis. X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution. The stalk linking the four SCR domains to the glycosylphosphatidylinositol anchor is extended by the addition of 11 highly charged O-glycans and positions the domains an estimated 177 A above the membrane. Mutation mapping and hydrophobic potential analysis suggest that the interaction with the convertase, and thus complement regulation, depends on the burial of a hydrophobic patch centered on the linker between SCR domains 2 and 3.
PubMed: 14734808
DOI: 10.1073/PNAS.0307200101
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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