1ok2

From Proteopedia

(Difference between revisions)

Current revision

Decay accelerating factor (CD55): the structure of an intact human complement regulator.

Structural highlights

1ok2 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DAF_HUMAN This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ward T, Pipkin PA, Clarkson NA, Stone DM, Minor PD, Almond JW. Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method. EMBO J. 1994 Nov 1;13(21):5070-4. PMID:7525274
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ok2"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ok2' size='340' side='right'caption='[[1ok2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ok2]] 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=1OK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OK2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ok2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OK2 FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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]], [[1ok3|1ok3]], [[1ok9|1ok9]], [[1uot|1uot]], [[1upn|1upn]]</div></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ok2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok2 OCA], [https://pdbe.org/1ok2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ok2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ok2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ok2 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/DAF_HUMAN DAF_HUMAN] This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.<ref>PMID:7525274</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Billington, J]]
+[[Category: Billington J]]
-[[Category: Crispin, M D.M]]
+[[Category: Crispin MDM]]
-[[Category: Dwek, R A]]
+[[Category: Dwek RA]]
-[[Category: Esser, D]]
+[[Category: Esser D]]
-[[Category: Evans, D J]]
+[[Category: Evans DJ]]
-[[Category: Lea, S M]]
+[[Category: Lea SM]]
-[[Category: Lukacik, P]]
+[[Category: Lukacik P]]
-[[Category: Morgan, B P]]
+[[Category: Morgan BP]]
-[[Category: Radcliffe, C M]]
+[[Category: Radcliffe CM]]
-[[Category: Roversi, P]]
+[[Category: Roversi P]]
-[[Category: Rudd, P M]]
+[[Category: Rudd PM]]
-[[Category: Smith, G P]]
+[[Category: Smith GP]]
-[[Category: Smith, R A.G]]
+[[Category: Smith RAG]]
-[[Category: White, J]]
+[[Category: White J]]
-[[Category: Williams, P A]]
+[[Category: Williams PA]]
-[[Category: Wormald, M R]]
+[[Category: Wormald MR]]
-[[Category: Decay acceleration of c3/c5 convertase]]
-[[Category: Pathogen receptor]]
-[[Category: Regulator of complement]]
-[[Category: Regulator of complement pathway]]
-[[Category: Short consensus repeat domain]]

1ok2

From Proteopedia

Current revision

Decay accelerating factor (CD55): the structure of an intact human complement regulator.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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