1ok3: Difference between revisions

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<StructureSection load='1ok3' size='340' side='right'caption='[[1ok3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1ok3' size='340' side='right'caption='[[1ok3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ok3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OK3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ok3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OK3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='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"><div style='overflow: auto; max-height: 3em;'>[[1h03|1h03]], [[1h04|1h04]], [[1h2p|1h2p]], [[1h2q|1h2q]], [[1m11|1m11]], [[1nwv|1nwv]], [[1ojv|1ojv]], [[1ojw|1ojw]], [[1ojy|1ojy]], [[1ok1|1ok1]], [[1ok2|1ok2]]</div></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ok3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok3 OCA], [https://pdbe.org/1ok3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ok3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ok3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ok3 ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==

Revision as of 10:14, 25 August 2021

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

1ok3 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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.

See Also

References

  1. ↑ 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. Complement regulation at the molecular level: the structure of decay-accelerating factor. Proc Natl Acad Sci U S A. 2004 Feb 3;101(5):1279-84. Epub 2004 Jan 20. PMID:14734808 doi:10.1073/pnas.0307200101

1ok3, resolution 2.20Å

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