2xrb: Difference between revisions
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<StructureSection load='2xrb' size='340' side='right'caption='[[2xrb]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2xrb' size='340' side='right'caption='[[2xrb]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xrb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</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]] 2.5Å</td></tr> | ||
<tr id=' | <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> | ||
== 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: Large Structures]] | [[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]] | ||
Latest revision as of 13:37, 20 December 2023
Structure of the N-terminal four domains of the complement regulator Rat CrryStructure of the N-terminal four domains of the complement regulator Rat Crry
Structural highlights
FunctionCR1L_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.[1] [2] [3] Publication Abstract from PubMedComplement receptor 1-related protein Y (CrrY) is an important cell-surface regulator of complement that is unique to rodent species. The structure of rat CrrY domains 1-4 has been determined in two distinct crystal forms and reveals a 70 degrees bend between domains 3 and 4. Comparisons of this structure with those of other complement regulators suggests that rearrangement of this interface may occur on forming the regulatory complex with C3b. Structures of the rat complement regulator CrrY.,Roversi P, Johnson S, Caesar JJ, McLean F, Leath KJ, Tsiftsoglou SA, Morgan BP, Harris CL, Sim RB, Lea SM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):739-43., Epub 2011 Jun 23. PMID:21795784[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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