1OK3

Decay accelerating factor (cd55): the structure of an intact human complement regulator.

Summary for 1OK3

• Entry DOI: 10.2210/pdb1ok3/pdb
• Related: 1H03 1H04 1H2P 1H2Q 1M11 1NWV 1OJV 1OJW 1OJY 1OK1 1OK2
• Descriptor: COMPLEMENT DECAY-ACCELERATING FACTOR, ACETATE ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: regulator of complement pathway, regulator of complement, decay acceleration of c3/c5 convertases, pathogen receptor, short consensus repeat domains
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 57794.06

Authors

Lukacik, P.,Roversi, P.,White, J.,Esser, D.,Smith, G.P.,Billington, J.,Williams, P.A.,Rudd, P.M.,Wormald, M.R.,Crispin, M.D.M.,Radcliffe, C.M.,Dwek, R.A.,Evans, D.J.,Morgan, B.P.,Smith, R.A.G.,Lea, S.M. (deposition date: 2003-07-16, release date: 2004-01-07, Last modification date: 2023-12-13)

Primary citation

Lukacik, 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

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)