1ok2

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[[Image:1ok2.gif|left|200px]]
[[Image:1ok2.gif|left|200px]]
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{{Structure
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|PDB= 1ok2 |SIZE=350|CAPTION= <scene name='initialview01'>1ok2</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1ok2", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ok2| PDB=1ok2 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ok2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok2 OCA], [http://www.ebi.ac.uk/pdbsum/1ok2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ok2 RCSB]</span>
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}}
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'''DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.'''
'''DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.'''
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[[Category: Williams, P.]]
[[Category: Williams, P.]]
[[Category: Wormald, M R.]]
[[Category: Wormald, M R.]]
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[[Category: decay acceleration of c3/c5 convertase]]
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[[Category: Decay acceleration of c3/c5 convertase]]
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[[Category: pathogen receptor]]
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[[Category: Pathogen receptor]]
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[[Category: regulator of complement]]
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[[Category: Regulator of complement]]
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[[Category: short consensus repeat domain]]
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[[Category: Short consensus repeat domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:56:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:30 2008''
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Revision as of 00:56, 3 May 2008

Template:STRUCTURE 1ok2

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


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.

About this Structure

1OK2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Sat May 3 03:56:57 2008

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