2xrd
From Proteopedia
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==Structure of the N-terminal four domains of the complement regulator Rat Crry== | ==Structure of the N-terminal four domains of the complement regulator Rat Crry== | ||
- | <StructureSection load='2xrd' size='340' side='right' caption='[[2xrd]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='2xrd' size='340' side='right'caption='[[2xrd]], [[Resolution|resolution]] 3.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2xrd]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2xrd]] 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=2XRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRD FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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=2xrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrd OCA], [https://pdbe.org/2xrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrd RCSB], [https://www.ebi.ac.uk/pdbsum/2xrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrd ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [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> | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Rattus norvegicus]] |
- | [[Category: | + | [[Category: Johnson S]] |
- | [[Category: | + | [[Category: Lea SM]] |
- | [[Category: | + | [[Category: Leath KJ]] |
- | [[Category: | + | [[Category: Morgan BP]] |
- | [[Category: | + | [[Category: Roversi P]] |
- | + |
Current revision
Structure of the N-terminal four domains of the complement regulator Rat Crry
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