1ok3: Difference between revisions
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==Decay accelerating factor (cd55): the structure of an intact human complement regulator.== | |||
<StructureSection load='1ok3' size='340' side='right' caption='[[1ok3]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1ok3' size='340' side='right' caption='[[1ok3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h03|1h03]], [[1h04|1h04]], [[1h2p|1h2p]], [[1h2q|1h2q]], [[1m11|1m11]], [[1nwv|1nwv]], [[1ojv|1ojv]], [[1ojw|1ojw]], [[1ojy|1ojy]], [[1ok1|1ok1]], [[1ok2|1ok2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h03|1h03]], [[1h04|1h04]], [[1h2p|1h2p]], [[1h2q|1h2q]], [[1m11|1m11]], [[1nwv|1nwv]], [[1ojv|1ojv]], [[1ojw|1ojw]], [[1ojy|1ojy]], [[1ok1|1ok1]], [[1ok2|1ok2]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ok3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok3 OCA], [http://pdbe.org/1ok3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ok3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ok3 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ok3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok3 OCA], [http://pdbe.org/1ok3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ok3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ok3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ok3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/1ok3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/1ok3_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:03, 7 February 2018
Decay accelerating factor (cd55): the structure of an intact human complement regulator.Decay accelerating factor (cd55): the structure of an intact human complement regulator.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Billington, J
- Crispin, M D.M
- Dwek, R A
- Esser, D
- Evans, D J
- Lea, S M
- Lukacik, P
- Morgan, B P
- Radcliffe, C M
- Roversi, P
- Rudd, P M
- Smith, G P
- Smith, R A.G
- White, J
- Williams, P A
- Wormald, M R
- Decay acceleration of c3/c5 convertase
- Pathogen receptor
- Regulator of complement
- Regulator of complement pathway
- Short consensus repeat domain