2xrd: Difference between revisions

Latest revision as of 10:37, 20 December 2023

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

Structural highlights

2xrd is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Antic Stankovic J, Vucevic D, Majstorovic I, Vasilijic S, Colic M. The role of rat Crry, a complement regulatory protein, in proliferation of thymocytes. Life Sci. 2004 Nov 5;75(25):3053-62. PMID:15474557 doi:10.1016/j.lfs.2004.06.007
↑ Quigg RJ, Holers VM, Morgan BP, Sneed AE 3rd. Crry and CD59 regulate complement in rat glomerular epithelial cells and are inhibited by the nephritogenic antibody of passive Heymann nephritis. J Immunol. 1995 Apr 1;154(7):3437-43 PMID:7534798
↑ Takizawa H, Okada N, Okada H. Complement inhibitor of rat cell membrane resembling mouse Crry/p65. J Immunol. 1994 Mar 15;152(6):3032-8 PMID:8144902
↑ Roversi P, Johnson S, Caesar JJ, McLean F, Leath KJ, Tsiftsoglou SA, Morgan BP, Harris CL, Sim RB, Lea SM. Structures of the rat complement regulator CrrY. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):739-43., Epub 2011 Jun 23. PMID:21795784 doi:https://dx.doi.org/10.1107/S1744309111016551

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OCA

[1] Antic Stankovic J, Vucevic D, Majstorovic I, Vasilijic S, Colic M. The role of rat Crry, a complement regulatory protein, in proliferation of thymocytes. Life Sci. 2004 Nov 5;75(25):3053-62. PMID:15474557 doi:10.1016/j.lfs.2004.06.007

[2] Quigg RJ, Holers VM, Morgan BP, Sneed AE 3rd. Crry and CD59 regulate complement in rat glomerular epithelial cells and are inhibited by the nephritogenic antibody of passive Heymann nephritis. J Immunol. 1995 Apr 1;154(7):3437-43 PMID:7534798

[3] Takizawa H, Okada N, Okada H. Complement inhibitor of rat cell membrane resembling mouse Crry/p65. J Immunol. 1994 Mar 15;152(6):3032-8 PMID:8144902

[4] Roversi P, Johnson S, Caesar JJ, McLean F, Leath KJ, Tsiftsoglou SA, Morgan BP, Harris CL, Sim RB, Lea SM. Structures of the rat complement regulator CrrY. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):739-43., Epub 2011 Jun 23. PMID:21795784 doi:https://dx.doi.org/10.1107/S1744309111016551

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@@ Line 3: / Line 3: @@
 <StructureSection load='2xrd' size='340' side='right'caption='[[2xrd]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xrd]] 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=2XRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRD FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ntj|1ntj]], [[2xrb|2xrb]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</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 ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Johnson, S]]
+[[Category: Rattus norvegicus]]
-[[Category: Lea, S M]]
+[[Category: Johnson S]]
-[[Category: Leath, K J]]
+[[Category: Lea SM]]
-[[Category: Morgan, B P]]
+[[Category: Leath KJ]]
-[[Category: Roversi, P]]
+[[Category: Morgan BP]]
-[[Category: Extracellular protein]]
+[[Category: Roversi P]]
-[[Category: Immune system]]

2xrd: Difference between revisions

Latest revision as of 10:37, 20 December 2023

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

Structural highlights

Function

Publication Abstract from PubMed

References

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