1h2p: Difference between revisions
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<StructureSection load='1h2p' size='340' side='right'caption='[[1h2p]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1h2p' size='340' side='right'caption='[[1h2p]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1h2p]] is a 1 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=1H2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2P FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=1h2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2p OCA], [https://pdbe.org/1h2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2p RCSB], [https://www.ebi.ac.uk/pdbsum/1h2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2p 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=1h2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2p OCA], [https://pdbe.org/1h2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2p RCSB], [https://www.ebi.ac.uk/pdbsum/1h2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Billington | [[Category: Billington J]] | ||
[[Category: Chaudhry | [[Category: Chaudhry Y]] | ||
[[Category: Evans | [[Category: Evans DJ]] | ||
[[Category: Goodfellow | [[Category: Goodfellow I]] | ||
[[Category: Lea | [[Category: Lea SM]] | ||
[[Category: Spiller | [[Category: Spiller B]] | ||
[[Category: Williams | [[Category: Williams P]] | ||
Revision as of 15:15, 13 December 2023
Human CD55 domains 3 & 4Human CD55 domains 3 & 4
Structural highlights
FunctionDAF_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 PubMedDecay-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 AlsoReferences
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