1ok2
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ok2.gif|left|200px]]<br /> | + | [[Image:1ok2.gif|left|200px]]<br /><applet load="1ok2" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ok2" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ok2, resolution 2.5Å" /> | caption="1ok2, resolution 2.5Å" /> | ||
'''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 /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1OK2 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]. | + | 1OK2 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=AC1:Gol Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK2 OCA]. |
==Reference== | ==Reference== | ||
| Line 41: | Line 40: | ||
[[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 Dec 18 17:48:01 2007'' |
Revision as of 15:38, 18 December 2007
|
DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.
Contents |
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.
Disease
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 Structure
1OK2 is a Single protein structure of sequence from Homo sapiens with ACT, SO4 and GOL as ligands. Known structural/functional Site: . 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 Tue Dec 18 17:48:01 2007
Categories: 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
