1h2q: Difference between revisions
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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 [ | <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'>[ | <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 == | ||
[[ | [[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]] | ||
Revision as of 14:31, 28 July 2021
Human CD55 domains 3 & 4Human CD55 domains 3 & 4
Structural highlights
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 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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