1h2p: Difference between revisions

Revision as of 12:15, 13 December 2023

Human CD55 domains 3 & 4

Structural highlights

1h2p is a 1 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 2.8Å
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.

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:https://dx.doi.org/10.1074/jbc.M212561200

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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:https://dx.doi.org/10.1074/jbc.M212561200

[1]

[2]

@@ Line 3: / Line 3: @@
 <StructureSection load='1h2p' size='340' side='right'caption='[[1h2p]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h2p]] 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=1H2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2P FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h03|1h03]], [[1h04|1h04]], [[1h2q|1h2q]], [[1m11|1m11]]</div></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]] 2.8&#8491;</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>
 == 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>
+[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 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Billington, J]]
+[[Category: Billington J]]
-[[Category: Chaudhry, Y]]
+[[Category: Chaudhry Y]]
-[[Category: Evans, D J]]
+[[Category: Evans DJ]]
-[[Category: Goodfellow, I]]
+[[Category: Goodfellow I]]
-[[Category: Lea, S M]]
+[[Category: Lea SM]]
-[[Category: Spiller, B]]
+[[Category: Spiller B]]
-[[Category: Williams, P]]
+[[Category: Williams P]]
-[[Category: Alternative splicing]]
-[[Category: Bacterial receptor]]
-[[Category: Complement decay accelerating factor]]
-[[Category: Complement pathway]]
-[[Category: Enteroviral receptor]]
-[[Category: Gpi-anchor]]
-[[Category: Immune system protein]]
-[[Category: Ligand for cd97]]

1h2p: Difference between revisions

Revision as of 12:15, 13 December 2023

Human CD55 domains 3 & 4

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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