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[[Image:2h3n.jpg|left|200px]]


{{Structure
==Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer==
|PDB= 2h3n |SIZE=350|CAPTION= <scene name='initialview01'>2h3n</scene>, resolution 2.3&Aring;
<StructureSection load='2h3n' size='340' side='right'caption='[[2h3n]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2h3n]] is a 4 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=2H3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H3N FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE= VPREB1, VPREB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), IGLL1, IGL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3n OCA], [https://pdbe.org/2h3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h3n RCSB], [https://www.ebi.ac.uk/pdbsum/2h3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h3n ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[2h32|2H32]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3n OCA], [http://www.ebi.ac.uk/pdbsum/2h3n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h3n RCSB]</span>
[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.
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/2h3n_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2h3n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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.


==About this Structure==
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>
2H3N is a [[Protein complex]] structure of sequences 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=2H3N OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/17431183 17431183]
</div>
<div class="pdbe-citations 2h3n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Bankovich, A J.]]
[[Category: Bankovich AJ]]
[[Category: Garcia, K C.]]
[[Category: Garcia KC]]
[[Category: beta sheet]]
[[Category: v- and c-type immunoglobulin fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:59 2008''

Latest revision as of 09:09, 6 November 2024

Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer

2h3n, resolution 2.30Å

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