2icc: Difference between revisions

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[[Image:2icc.png|left|200px]]


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==Extracellular Domain of CRIg==
The line below this paragraph, containing "STRUCTURE_2icc", creates the "Structure Box" on the page.
<StructureSection load='2icc' size='340' side='right'caption='[[2icc]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2icc]] 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=2ICC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ICC FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2icc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2icc OCA], [https://pdbe.org/2icc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2icc RCSB], [https://www.ebi.ac.uk/pdbsum/2icc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2icc ProSAT]</span></td></tr>
{{STRUCTURE_2icc|  PDB=2icc  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/VSIG4_HUMAN VSIG4_HUMAN] Phagocytic receptor, strong negative regulator of T-cell proliferation and IL2 production. Potent inhibitor of the alternative complement pathway convertases.<ref>PMID:17016562</ref> <ref>PMID:17051150</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/ic/2icc_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=2icc ConSurf].
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== Publication Abstract from PubMed ==
The complement system is a key part of the innate immune system, and is required for clearance of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles, but it is unknown how CRIg selectively recognizes proteolytic C3-fragments and whether binding of CRIg to C3b inhibits convertase activation. Here we present the crystal structure of C3b in complex with CRIg and, using CRIg mutants, provide evidence that CRIg acts as an inhibitor of the alternative pathway of complement. The structure shows that activation of C3 induces major structural rearrangements, including a dramatic movement (&gt;80 A) of the thioester-bond-containing domain through which C3b attaches to pathogen surfaces. We show that CRIg is not only a phagocytic receptor, but also a potent inhibitor of the alternative pathway convertases. The structure provides insights into the complex macromolecular structural rearrangements that occur during complement activation and inhibition. Moreover, our structure-function studies relating the structural basis of complement activation and the means by which CRIg inhibits the convertases provide important clues to the development of therapeutics that target complement.


===Extracellular Domain of CRIg===
Structure of C3b in complex with CRIg gives insights into regulation of complement activation.,Wiesmann C, Katschke KJ, Yin J, Helmy KY, Steffek M, Fairbrother WJ, McCallum SA, Embuscado L, DeForge L, Hass PE, van Lookeren Campagne M Nature. 2006 Nov 9;444(7116):217-20. Epub 2006 Oct 15. PMID:17051150<ref>PMID:17051150</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 17051150 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17051150}}
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</StructureSection>
==About this Structure==
2ICC is a 1 chain 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=2ICC OCA].
 
==Reference==
<ref group="xtra">PMID:17051150</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Wiesmann, C.]]
[[Category: Large Structures]]
[[Category: Alternative pathway]]
[[Category: Wiesmann C]]
[[Category: Complement receptor]]
[[Category: Ig like domain]]
[[Category: Immune system]]
 
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