2h32

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{{STRUCTURE_2h32| PDB=2h32 | SCENE= }}
 
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===Crystal structure of the pre-B cell receptor===
 
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{{ABSTRACT_PUBMED_17431183}}
 
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==Disease==
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==Crystal structure of the pre-B cell receptor==
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[[http://www.uniprot.org/uniprot/IGLL1_HUMAN IGLL1_HUMAN]] Defects in IGLL1 are the cause of agammaglobulinemia type 2 (AGM2) [MIM:[http://omim.org/entry/613500 613500]]. 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.
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<StructureSection load='2h32' size='340' side='right'caption='[[2h32]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2h32]] is a 3 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=2H32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H32 FirstGlance]. <br>
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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]] 2.7&#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=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=2h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h32 OCA], [https://pdbe.org/2h32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h32 RCSB], [https://www.ebi.ac.uk/pdbsum/2h32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h32 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VPREB_HUMAN VPREB_HUMAN] Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation.
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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/h3/2h32_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2h32 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 pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell development. In the 2.7 angstrom structure of a human pre-BCR Fab-like fragment, consisting of an antibody heavy chain (HC) paired with the surrogate light chain, the "unique regions" of VpreB and lambda5 replace the complementarity-determining region 3 (CDR3) loop of an antibody light chain and appear to "probe" the HC CDR3, potentially influencing the selection of the antibody repertoire. Biochemical analysis indicates that the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling mechanism.
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==Function==
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Structural insight into pre-B cell receptor function.,Bankovich AJ, Raunser S, Juo ZS, Walz T, Davis MM, Garcia KC Science. 2007 Apr 13;316(5822):291-4. PMID:17431183<ref>PMID:17431183</ref>
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[[http://www.uniprot.org/uniprot/VPREB_HUMAN VPREB_HUMAN]] Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation. [[http://www.uniprot.org/uniprot/IGLL1_HUMAN IGLL1_HUMAN]] Critical for B-cell development.<ref>PMID:9419212</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2h32]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H32 OCA].
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</div>
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<div class="pdbe-citations 2h32" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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<ref group="xtra">PMID:017431183</ref><references group="xtra"/><references/>
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bankovich, A J.]]
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[[Category: Large Structures]]
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[[Category: Beta sheet]]
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[[Category: Bankovich AJ]]
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[[Category: Immune system]]
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[[Category: V and c-type ig fold]]
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Current revision

Crystal structure of the pre-B cell receptor

PDB ID 2h32

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