3kho

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{{Seed}}
 
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[[Image:3kho.jpg|left|200px]]
 
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==Crystal structure of murine Ig-beta (CD79b) homodimer==
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The line below this paragraph, containing "STRUCTURE_3kho", creates the "Structure Box" on the page.
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<StructureSection load='3kho' size='340' side='right'caption='[[3kho]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3kho]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KHO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.11&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_3kho| PDB=3kho | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kho OCA], [https://pdbe.org/3kho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kho RCSB], [https://www.ebi.ac.uk/pdbsum/3kho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kho ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CD79B_MOUSE CD79B_MOUSE] 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:8175787</ref> <ref>PMID:10352267</ref> <ref>PMID:12356683</ref> <ref>PMID:15661879</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/3kho_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kho ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of murine Ig-beta (CD79b) homodimer===
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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<ref>PMID:20696394</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20696394}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3kho" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20696394 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20696394}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3KHO is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KHO OCA].
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==Reference==
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<ref group="xtra">PMID:20696394</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Radaev, S.]]
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[[Category: Radaev S]]
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[[Category: Sun, P D.]]
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[[Category: Sun PD]]
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[[Category: Bcr]]
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[[Category: Cd79a]]
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[[Category: Cd79b]]
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[[Category: Ig domain]]
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[[Category: Ig-beta]]
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[[Category: Immunoglobulin domain]]
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[[Category: Protein binding]]
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[[Category: V-set]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 25 08:55:49 2010''
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Current revision

Crystal structure of murine Ig-beta (CD79b) homodimer

PDB ID 3kho

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