1ok3: Difference between revisions
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[[Image:1ok3.gif|left|200px]]<br /><applet load="1ok3" size=" | [[Image:1ok3.gif|left|200px]]<br /><applet load="1ok3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ok3, resolution 2.2Å" /> | caption="1ok3, resolution 2.2Å" /> | ||
'''DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.'''<br /> | '''DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OK3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACT, SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=G1:Glycosylation Site'>G1</scene>. Full crystallographic information is available from [http:// | 1OK3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=G1:Glycosylation+Site'>G1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: short consensus repeat domains]] | [[Category: short consensus repeat domains]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:59:09 2008'' | ||
Revision as of 10:59, 3 February 2008
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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.
DiseaseDisease
Known diseases associated with this structure: Blood group Cromer OMIM:[125240], Blood group, Knops system OMIM:[120620], CR1 deficiency OMIM:[120620], Malaria, severe, resistance to OMIM:[120620], SLE susceptibility OMIM:[120620]
About this StructureAbout this Structure
1OK3 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Known structural/functional Site: . 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
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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.
- ACT
- GOL
- SO4
- Decay acceleration of c3/c5 convertases
- Pathogen receptor
- Regulator of complement
- Short consensus repeat domains