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| | <StructureSection load='1h2q' size='340' side='right'caption='[[1h2q]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1h2q' size='340' side='right'caption='[[1h2q]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h2q]] is a 1 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=1H2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h2q]] is a 1 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=1H2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2Q FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h03|1h03]], [[1h04|1h04]], [[1h2p|1h2p]], [[1m11|1m11]], [[1nwv|1nwv]], [[1ojv|1ojv]], [[1ojw|1ojw]], [[1ojy|1ojy]], [[1ok1|1ok1]], [[1ok2|1ok2]], [[1ok3|1ok3]], [[1ok9|1ok9]], [[1uot|1uot]]</td></tr> | + | </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]], [[1m11|1m11]], [[1nwv|1nwv]], [[1ojv|1ojv]], [[1ojw|1ojw]], [[1ojy|1ojy]], [[1ok1|1ok1]], [[1ok2|1ok2]], [[1ok3|1ok3]], [[1ok9|1ok9]], [[1uot|1uot]]</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=1h2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2q OCA], [http://pdbe.org/1h2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h2q RCSB], [http://www.ebi.ac.uk/pdbsum/1h2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2q 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=1h2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2q OCA], [https://pdbe.org/1h2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2q RCSB], [https://www.ebi.ac.uk/pdbsum/1h2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
1h2q is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Related: | 1h03, 1h04, 1h2p, 1m11, 1nwv, 1ojv, 1ojw, 1ojy, 1ok1, 1ok2, 1ok3, 1ok9, 1uot |
| 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
Decay-accelerating factor (CD55), a regulator of the alternative and classical pathways of complement activation, is expressed on all serum-exposed cells. It is used by pathogens, including many enteroviruses and uropathogenic Escherichia coli, as a receptor prior to infection. We describe the x-ray structure of a pathogen-binding fragment of human CD55 at 1.7 A resolution containing two of the three domains required for regulation of human complement. We have used mutagenesis to map biological functions onto the molecule; decay-accelerating activity maps to a single face of the molecule, whereas bacterial and viral pathogens recognize a variety of different sites on CD55.
Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A.,Williams P, Chaudhry Y, Goodfellow IG, Billington J, Powell R, Spiller OB, Evans DJ, Lea S J Biol Chem. 2003 Mar 21;278(12):10691-6. Epub 2002 Dec 22. PMID:12499389[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Williams P, Chaudhry Y, Goodfellow IG, Billington J, Powell R, Spiller OB, Evans DJ, Lea S. Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A. J Biol Chem. 2003 Mar 21;278(12):10691-6. Epub 2002 Dec 22. PMID:12499389 doi:http://dx.doi.org/10.1074/jbc.M212561200
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