2LKQ

NMR structure of the lambda 5 22-45 peptide

Summary for 2LKQ

• Entry DOI: 10.2210/pdb2lkq/pdb
• NMR Information: BMRB: 18009
• Descriptor: Immunoglobulin lambda-like polypeptide 1 (1 entity in total)
• Functional Keywords: pre-bcr, b cell development, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P15814
• Total number of polymer chains: 1
• Total formula weight: 2856.28

Authors

Elantak, L.,Espeli, M.,Boned, A.,Bornet, O.,Breton, C.,Feracci, M.,Roche, P.,Guerlesquin, F.,Schiff, C. (deposition date: 2011-10-19, release date: 2012-10-24, Last modification date: 2024-05-15)

Primary citation

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., 287:44703-44713, 2012

PubMed Abstract: During B cell differentiation in the bone marrow, the expression and activation of the pre-B cell receptor (pre-BCR) constitute crucial checkpoints for B cell development. Both constitutive and ligand-dependent pre-BCR activation modes have been described. The pre-BCR constitutes an immunoglobulin heavy chain (Igμ) and a surrogate light chain composed of the invariant λ5 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 λ5 (λ5-UR). Here, we investigated the solution structure of a minimal λ5-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. We identified key hydrophobic residues from the λ5-UR as crucial for the interaction with GAL1 and for pre-BCR clustering. These residues involved in GAL1-induced pre-BCR activation are different from those essential for autonomous receptor activation. Overall, our results indicate that constitutive and ligand-induced pre-BCR activation could occur in a complementary manner.

PubMed: 23124203
DOI: 10.1074/jbc.M112.395152

Experimental method

SOLUTION NMR