1ok2

DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.

spinqualitylabelsall models 1ok2, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ok2 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, GOL, SO4 Related: 1h03, 1h04, 1h2p, 1h2q, 1m11, 1nwv, 1ojv, 1ojw, 1ojy, 1ok1, 1ok3, 1ok9, 1uot, 1upn Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Complement regulation at the molecular level: the structure of decay-accelerating factor.,Lukacik P, Roversi P, White J, Esser D, Smith GP, Billington J, Williams PA, Rudd PM, Wormald MR, Harvey DJ, Crispin MD, Radcliffe CM, Dwek RA, Evans DJ, Morgan BP, Smith RA, Lea SM Proc Natl Acad Sci U S A. 2004 Feb 3;101(5):1279-84. Epub 2004 Jan 20. PMID:14734808 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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