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| | ==Crystal structure of human Ig-beta homodimer== | | ==Crystal structure of human Ig-beta homodimer== |
| - | <StructureSection load='3kg5' size='340' side='right' caption='[[3kg5]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='3kg5' size='340' side='right'caption='[[3kg5]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3kg5]] is a 2 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=3KG5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KG5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3kg5]] is a 2 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=3KG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KG5 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B29, CD79B, IGB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 3.2Å</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=3kg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg5 OCA], [http://pdbe.org/3kg5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kg5 RCSB], [http://www.ebi.ac.uk/pdbsum/3kg5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kg5 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=3kg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg5 OCA], [https://pdbe.org/3kg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kg5 RCSB], [https://www.ebi.ac.uk/pdbsum/3kg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kg5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/CD79B_HUMAN CD79B_HUMAN]] Autosomal agammaglobulinemia. Defects in CD79B are the cause of agammaglobulinemia type 6 (AGM6) [MIM:[http://omim.org/entry/612692 612692]]. It is a primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.<ref>PMID:17675462</ref> | + | [https://www.uniprot.org/uniprot/CD79B_HUMAN CD79B_HUMAN] Autosomal agammaglobulinemia. Defects in CD79B are the cause of agammaglobulinemia type 6 (AGM6) [MIM:[https://omim.org/entry/612692 612692]. It is a primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.<ref>PMID:17675462</ref> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CD79B_HUMAN CD79B_HUMAN]] Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.<ref>PMID:8617796</ref> <ref>PMID:9057631</ref> <ref>PMID:12097390</ref> | + | [https://www.uniprot.org/uniprot/CD79B_HUMAN CD79B_HUMAN] Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.<ref>PMID:8617796</ref> <ref>PMID:9057631</ref> <ref>PMID:12097390</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/3kg5_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/3kg5_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> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Radaev, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Sun, P D]] | + | [[Category: Radaev S]] |
| - | [[Category: Bcr]] | + | [[Category: Sun PD]] |
| - | [[Category: Cd79b]]
| + | |
| - | [[Category: Ig-beta]]
| + | |
| - | [[Category: Immunoglobulin domain]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Disease
CD79B_HUMAN Autosomal agammaglobulinemia. Defects in CD79B are the cause of agammaglobulinemia type 6 (AGM6) [MIM:612692. It is a primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.[1]
Function
CD79B_HUMAN Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.[2] [3] [4]
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
The B cell antigen receptor (BCR) plays an essential role in all phases of B cell development. Here we show that the extracellular domains of murine and human Igbeta form an I-set immunoglobulin-like structure with an interchain disulfide between cysteines on their G strands. Structural and sequence analysis suggests that Igalpha displays a similar fold as Igbeta. An Igalphabeta heterodimer model was generated based on the unique disulfide-bonded Igbeta dimer. Solution binding studies showed that the extracellular domains of Igalphabeta preferentially recognize the constant region of BCR with mu chain specificity, suggesting a role for Igalphabeta to enhance BCRmu chain signaling. Cluster mutations on Igalpha, Igbeta, and a membrane-bound form of immunoglobulin (mIgM) based on the structural model identified distinct areas of potential contacts involving charged residues on both subunits of the coreceptor and the Cmu4 domain of mIgM. These studies provide the first structural model for understanding BCR function.
Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor.,Radaev S, Zou Z, Tolar P, Nguyen K, Nguyen A, Krueger PD, Stutzman N, Pierce S, Sun PD Structure. 2010 Aug 11;18(8):934-43. PMID:20696394[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dobbs AK, Yang T, Farmer D, Kager L, Parolini O, Conley ME. Cutting edge: a hypomorphic mutation in Igbeta (CD79b) in a patient with immunodeficiency and a leaky defect in B cell development. J Immunol. 2007 Aug 15;179(4):2055-9. PMID:17675462
- ↑ Luisiri P, Lee YJ, Eisfelder BJ, Clark MR. Cooperativity and segregation of function within the Ig-alpha/beta heterodimer of the B cell antigen receptor complex. J Biol Chem. 1996 Mar 1;271(9):5158-63. PMID:8617796
- ↑ Tseng J, Eisfelder BJ, Clark MR. B-cell antigen receptor-induced apoptosis requires both Ig alpha and Ig beta. Blood. 1997 Mar 1;89(5):1513-20. PMID:9057631
- ↑ Pelanda R, Braun U, Hobeika E, Nussenzweig MC, Reth M. B cell progenitors are arrested in maturation but have intact VDJ recombination in the absence of Ig-alpha and Ig-beta. J Immunol. 2002 Jul 15;169(2):865-72. PMID:12097390
- ↑ Radaev S, Zou Z, Tolar P, Nguyen K, Nguyen A, Krueger PD, Stutzman N, Pierce S, Sun PD. Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor. Structure. 2010 Aug 11;18(8):934-43. PMID:20696394 doi:10.1016/j.str.2010.04.019
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