View source for 2lkq


==NMR structure of the lambda 5 22-45 peptide==
<StructureSection load='2lkq' size='340' side='right'caption='[[2lkq]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lkq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkq OCA], [https://pdbe.org/2lkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkq RCSB], [https://www.ebi.ac.uk/pdbsum/2lkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkq ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/IGLL1_HUMAN IGLL1_HUMAN] Defects in IGLL1 are the cause of agammaglobulinemia type 2 (AGM2) [MIM:[https://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.
== Function ==
[https://www.uniprot.org/uniprot/IGLL1_HUMAN IGLL1_HUMAN] Critical for B-cell development.<ref>PMID:9419212</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During B cell differentiation in the bone marrow, the expression and activation of the pre-B cell receptor (pre-BCR) constitutes a crucial checkpoint for B cell development. Both constitutive and ligand-dependent pre-BCR activation modes have been described. The pre-BCR is constituted of an immunoglobulin heavy chain (Igmu) and of a surrogate light chain (SLC) composed of the invariant lambda5 and VpreB proteins. We previously showed that Galectin-1 (GAL1), produced by bone marrow stromal cells, is a pre-BCR ligand that induces receptor clustering, leading to efficient pre-BII cell proliferation and differentiation. GAL1 interacts with the pre-BCR via the unique region of lambda5 (lambda5-UR). Here we investigated the solution structure of a minimal lambda5-UR motif that interacts with GAL1. This motif adopts a stable helical conformation that docks onto a GAL1 hydrophobic surface adjacent to its carbohydrate-binding site (CBS). We identified key hydrophobic residues from the lambda5-UR as crucial for the interaction with GAL1 and for pre-BCR clustering. These residues involved in GAL1-induced pre-BCR activation are different to those essential for autonomous receptor activation. Overall, our results indicate that constitutive and ligand-induced pre-BCR activation could occur in a complementary manner.

Structural basis for galectin-1-dependent pre-B cell receptor (pre-BCR) activation.,Elantak L, Espeli M, Boned A, Bornet O, Bonzi J, Gauthier L, Feracci M, Roche P, Guerlesquin F, Schiff C J Biol Chem. 2012 Nov 2. PMID:23124203<ref>PMID:23124203</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lkq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Boned A]]
[[Category: Bornet O]]
[[Category: Breton C]]
[[Category: Elantak L]]
[[Category: Espeli M]]
[[Category: Feracci M]]
[[Category: Guerlesquin F]]
[[Category: Roche P]]
[[Category: Schiff C]]