1ok9: Difference between revisions
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|PDB= 1ok9 |SIZE=350|CAPTION= <scene name='initialview01'>1ok9</scene>, resolution 3.0Å | |PDB= 1ok9 |SIZE=350|CAPTION= <scene name='initialview01'>1ok9</scene>, resolution 3.0Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ok9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok9 OCA], [http://www.ebi.ac.uk/pdbsum/1ok9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ok9 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Williams, P.]] | [[Category: Williams, P.]] | ||
[[Category: Wormald, M R.]] | [[Category: Wormald, M R.]] | ||
[[Category: decay acceleration of c3/c5 convertase]] | [[Category: decay acceleration of c3/c5 convertase]] | ||
[[Category: immune system protein]] | [[Category: immune system protein]] | ||
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[[Category: short consensus repeat domain]] | [[Category: short consensus repeat domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:32 2008'' | ||
Revision as of 22:46, 30 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.
OverviewOverview
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.
About this StructureAbout this Structure
1OK9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Mar 30 22:46:32 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Single protein
- Billington, J.
- Crispin, M.
- Dwek, R A.
- Esser, D.
- Evans, D J.
- Lea, S M.
- Lukacik, P.
- Morgan, B P.
- Radcliffe, C M.
- Roversi, P.
- Rudd, P.
- Smith, G P.
- Smith, R A.G.
- White, J.
- Williams, P.
- Wormald, M R.
- Decay acceleration of c3/c5 convertase
- Immune system protein
- Pathogen receptor
- Regulator of complement
- Short consensus repeat domain