1ok3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 8: Line 8:


==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]]. Structure known Active Site: G1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK3 OCA]].  
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]. Structure known Active Site: G1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK3 OCA].  


==Reference==
==Reference==
Line 38: Line 38:
[[Category: short consensus repeat domains]]
[[Category: short consensus repeat domains]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:56:57 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 13:31:25 2007''

Revision as of 14:26, 5 November 2007

File:1ok3.gif


1ok3, resolution 2.2Å

Drag the structure with the mouse to rotate

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

1OK3 is a Single protein structure of sequence from Homo sapiens with ACT, SO4 and GOL as ligands. Structure known Active Site: G1. 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 Mon Nov 5 13:31:25 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA