2xrb

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Current revision (10:37, 20 December 2023) (edit) (undo)
 
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<StructureSection load='2xrb' size='340' side='right'caption='[[2xrb]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2xrb' size='340' side='right'caption='[[2xrb]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xrb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xrb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ntj|1ntj]], [[2xrd|2xrd]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2xrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrb OCA], [https://pdbe.org/2xrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrb RCSB], [https://www.ebi.ac.uk/pdbsum/2xrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrb 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=2xrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrb OCA], [https://pdbe.org/2xrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrb RCSB], [https://www.ebi.ac.uk/pdbsum/2xrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrb ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CR1L_RAT CR1L_RAT] Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. Also acts as a decay-accelerating factor, preventing the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Seems to act as a costimulatory factor for T-cells. May play a crucial role in early embryonic development by maintaining fetomaternal tolerance.<ref>PMID:15474557</ref> <ref>PMID:7534798</ref> <ref>PMID:8144902</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Johnson, S]]
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[[Category: Rattus norvegicus]]
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[[Category: Lea, S M]]
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[[Category: Johnson S]]
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[[Category: Leath, K J]]
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[[Category: Lea SM]]
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[[Category: Morgan, B P]]
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[[Category: Leath KJ]]
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[[Category: Roversi, P]]
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[[Category: Morgan BP]]
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[[Category: Immune system]]
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[[Category: Roversi P]]
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[[Category: Immunology]]
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Current revision

Structure of the N-terminal four domains of the complement regulator Rat Crry

PDB ID 2xrb

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