1ok9: Difference between revisions
New page: left|200px<br /> <applet load="1ok9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ok9, resolution 3.0Å" /> '''DECAY ACCELERATING F... |
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==About this Structure== | ==About this Structure== | ||
1OK9 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, PT, CL, SO4 and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK9 OCA]]. | 1OK9 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, PT, CL, SO4 and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK9 OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: short consensus repeat domains]] | [[Category: short consensus repeat domains]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:49:20 2007'' | ||
Revision as of 12:44, 30 October 2007
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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.
About this StructureAbout this Structure
1OK9 is a [Single protein] structure of sequence from [Homo sapiens] with ACT, PT, CL, SO4 and GOL as [ligands]. Structure known Active Site: AC1. 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
- CL
- GOL
- PT
- SO4
- Decay acceleration of c3/c5 convertases
- Immune system protein
- Pathogen receptor
- Regulator of complement
- Short consensus repeat domains