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| | ==NMR structure of the lambda 5 22-45 peptide== | | ==NMR structure of the lambda 5 22-45 peptide== |
| - | <StructureSection load='2lkq' size='340' side='right' caption='[[2lkq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lkq' size='340' side='right'caption='[[2lkq]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lkq]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKQ FirstGlance]. <br> | + | <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='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=2lkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkq OCA], [http://pdbe.org/2lkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lkq RCSB], [http://www.ebi.ac.uk/pdbsum/2lkq PDBsum]</span></td></tr> | + | </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> | | </table> |
| | == Disease == | | == Disease == |
| - | [[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. | + | [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 == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IGLL1_HUMAN IGLL1_HUMAN]] Critical for B-cell development.<ref>PMID:9419212</ref> | + | [https://www.uniprot.org/uniprot/IGLL1_HUMAN IGLL1_HUMAN] Critical for B-cell development.<ref>PMID:9419212</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Boned, A]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Bornet, O]] | + | [[Category: Large Structures]] |
| - | [[Category: Breton, C]] | + | [[Category: Boned A]] |
| - | [[Category: Elantak, L]] | + | [[Category: Bornet O]] |
| - | [[Category: Espeli, M]] | + | [[Category: Breton C]] |
| - | [[Category: Feracci, M]] | + | [[Category: Elantak L]] |
| - | [[Category: Guerlesquin, F]] | + | [[Category: Espeli M]] |
| - | [[Category: Roche, P]] | + | [[Category: Feracci M]] |
| - | [[Category: Schiff, C]] | + | [[Category: Guerlesquin F]] |
| - | [[Category: B cell development]]
| + | [[Category: Roche P]] |
| - | [[Category: Immune system]]
| + | [[Category: Schiff C]] |
| - | [[Category: Pre-bcr]]
| + | |
| Structural highlights
Disease
IGLL1_HUMAN Defects in IGLL1 are the cause of agammaglobulinemia type 2 (AGM2) [MIM: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
IGLL1_HUMAN Critical for B-cell development.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Minegishi Y, Coustan-Smith E, Wang YH, Cooper MD, Campana D, Conley ME. Mutations in the human lambda5/14.1 gene result in B cell deficiency and agammaglobulinemia. J Exp Med. 1998 Jan 5;187(1):71-7. PMID:9419212
- ↑ Elantak L, Espeli M, Boned A, Bornet O, Bonzi J, Gauthier L, Feracci M, Roche P, Guerlesquin F, Schiff C. Structural basis for galectin-1-dependent pre-B cell receptor (pre-BCR) activation. J Biol Chem. 2012 Nov 2. PMID:23124203 doi:http://dx.doi.org/10.1074/jbc.M112.395152
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