1ly2

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of unliganded human CD21 SCR1-SCR2 (Complement receptor type 2)

Structural highlights

1ly2 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CR2_HUMAN Genetic variations in CR2 are associated with susceptibility to systemic lupus erythematosus type 9 (SLEB9) [MIM:610927. Systemic lupus erythematosus (SLE) is a chronic autoimmune disease with a complex genetic basis. SLE is an inflammatory, and often febrile multisystemic disorder of connective tissue characterized principally by involvement of the skin, joints, kidneys, and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system.^[1] Defects in CR2 are the cause of immunodeficiency, common variable, type 7 (CVID7) [MIM:614699. A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B cells is usually in the normal range, but can be low.^[2]

Function

CR2_HUMAN Receptor for complement C3Dd, for the Epstein-Barr virus on human B-cells and T-cells and for HNRPU. Participates in B lymphocytes activation.^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human complement receptor type 2 (CD21) is the cellular receptor for Epstein-Barr virus (EBV), a human tumor virus. The N-terminal two short consensus repeats (SCR1-SCR2) of the receptor interact with the EBV glycoprotein gp350/220 and also with the natural CD21 ligand C3d. Here we present the crystal structure of the CD21 SCR1-SCR2 fragment in the absence of ligand and demonstrate that it is able to bind EBV. Based on a functional analysis of wild-type and mutant CD21 and molecular modeling, we identify a likely region for EBV attachment and demonstrate that this region is not involved in the interaction with C3d. A comparison with the previously determined structure of CD21 SCR1-SCR2 in complex with C3d shows that, in both cases, CD21 assumes compact V-shaped conformations. However, our analysis reveals a surprising degree of flexibility at the SCR1-SCR2 interface, suggesting interactions between the two domains are not specific. We present evidence that the V-shaped conformation is induced by deglycosylation of the protein, and that physiologic glycosylation of CD21 would result in a more extended conformation, perhaps with additional epitopes for C3d binding.

The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding.,Prota AE, Sage DR, Stehle T, Fingeroth JD Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10641-6. Epub 2002 Jul 16. PMID:12122212^[4]

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

References

↑ Wu H, Boackle SA, Hanvivadhanakul P, Ulgiati D, Grossman JM, Lee Y, Shen N, Abraham LJ, Mercer TR, Park E, Hebert LA, Rovin BH, Birmingham DJ, Chang DM, Chen CJ, McCurdy D, Badsha HM, Thong BY, Chng HH, Arnett FC, Wallace DJ, Yu CY, Hahn BH, Cantor RM, Tsao BP. Association of a common complement receptor 2 haplotype with increased risk of systemic lupus erythematosus. Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3961-6. Epub 2007 Feb 22. PMID:17360460 doi:0609101104
↑ Thiel J, Kimmig L, Salzer U, Grudzien M, Lebrecht D, Hagena T, Draeger R, Volxen N, Bergbreiter A, Jennings S, Gutenberger S, Aichem A, Illges H, Hannan JP, Kienzler AK, Rizzi M, Eibel H, Peter HH, Warnatz K, Grimbacher B, Rump JA, Schlesier M. Genetic CD21 deficiency is associated with hypogammaglobulinemia. J Allergy Clin Immunol. 2012 Mar;129(3):801-810.e6. doi:, 10.1016/j.jaci.2011.09.027. Epub 2011 Oct 27. PMID:22035880 doi:10.1016/j.jaci.2011.09.027
↑ Barel M, Balbo M, Gauffre A, Frade R. Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein. Mol Immunol. 1995 Apr;32(6):389-97. PMID:7753047
↑ Prota AE, Sage DR, Stehle T, Fingeroth JD. The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding. Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10641-6. Epub 2002 Jul 16. PMID:12122212 doi:10.1073/pnas.162360499

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ly2"

@@ Line 1: / Line 1: @@
 ==Crystal structure of unliganded human CD21 SCR1-SCR2 (Complement receptor type 2)==
-<StructureSection load='1ly2' size='340' side='right' caption='[[1ly2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1ly2' size='340' side='right'caption='[[1ly2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ly2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LY2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ly2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LY2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 1.8&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ly2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ly2 OCA], [http://pdbe.org/1ly2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ly2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ly2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ly2 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=1ly2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ly2 OCA], [https://pdbe.org/1ly2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ly2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ly2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ly2 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CR2_HUMAN CR2_HUMAN]] Genetic variations in CR2 are associated with susceptibility to systemic lupus erythematosus type 9 (SLEB9) [MIM:[http://omim.org/entry/610927 610927]]. Systemic lupus erythematosus (SLE) is a chronic autoimmune disease with a complex genetic basis. SLE is an inflammatory, and often febrile multisystemic disorder of connective tissue characterized principally by involvement of the skin, joints, kidneys, and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system.<ref>PMID:17360460</ref>   Defects in CR2 are the cause of immunodeficiency, common variable, type 7 (CVID7) [MIM:[http://omim.org/entry/614699 614699]]. A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B cells is usually in the normal range, but can be low.<ref>PMID:22035880</ref>
+[https://www.uniprot.org/uniprot/CR2_HUMAN CR2_HUMAN] Genetic variations in CR2 are associated with susceptibility to systemic lupus erythematosus type 9 (SLEB9) [MIM:[https://omim.org/entry/610927 610927]. Systemic lupus erythematosus (SLE) is a chronic autoimmune disease with a complex genetic basis. SLE is an inflammatory, and often febrile multisystemic disorder of connective tissue characterized principally by involvement of the skin, joints, kidneys, and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system.<ref>PMID:17360460</ref>   Defects in CR2 are the cause of immunodeficiency, common variable, type 7 (CVID7) [MIM:[https://omim.org/entry/614699 614699]. A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B cells is usually in the normal range, but can be low.<ref>PMID:22035880</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/CR2_HUMAN CR2_HUMAN]] Receptor for complement C3Dd, for the Epstein-Barr virus on human B-cells and T-cells and for HNRPU. Participates in B lymphocytes activation.<ref>PMID:7753047</ref>
+[https://www.uniprot.org/uniprot/CR2_HUMAN CR2_HUMAN] Receptor for complement C3Dd, for the Epstein-Barr virus on human B-cells and T-cells and for HNRPU. Participates in B lymphocytes activation.<ref>PMID:7753047</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 17: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ly/1ly2_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Fingeroth, J D]]
+[[Category: Large Structures]]
-[[Category: Prota, A E]]
+[[Category: Fingeroth JD]]
-[[Category: Sage, D R]]
+[[Category: Prota AE]]
-[[Category: Stehle, T]]
+[[Category: Sage DR]]
-[[Category: Complement control protein]]
+[[Category: Stehle T]]
-[[Category: Complement receptor]]
-[[Category: Epstein barr virus]]
-[[Category: Immune system]]
-[[Category: Regulator of complement activation]]
-[[Category: Short consensus repeat]]
-[[Category: Viral receptor]]

1ly2

From Proteopedia

Current revision

Crystal structure of unliganded human CD21 SCR1-SCR2 (Complement receptor type 2)

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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