2xrd: Difference between revisions
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New page: '''Unreleased structure''' The entry 2xrd is ON HOLD Authors: Leath, K.J., Roversi, P., Johnson, S., Morgan, B.P., Lea, S.M. Description: Structure of the N-terminal four domains of th... |
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==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=''> | |||
== Structural highlights == | |||
<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='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'>[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> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
Complement 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<ref>PMID:21795784</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xrd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Johnson S]] | |||
[[Category: Lea SM]] | |||
[[Category: Leath KJ]] | |||
[[Category: Morgan BP]] | |||
[[Category: Roversi P]] | |||
Latest revision as of 10:37, 20 December 2023
Structure of the N-terminal four domains of the complement regulator Rat Crry
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