1h2p: Difference between revisions

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[[Image:1h2p.gif|left|200px]]
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{{STRUCTURE_1h2p|  PDB=1h2p  |  SCENE=  }}
'''HUMAN CD55 DOMAINS 3 & 4'''


==Human CD55 domains 3 & 4==
<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/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='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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/1h2p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h2p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:12499389</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1H2P is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 1h2p" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12499389 12499389]
*[[CD55|CD55]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[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: Ligand for cd97]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:21:11 2008''
Retrieved from "https://proteopedia.org/1h2p"