2H3N

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

Summary for 2H3N

• Entry DOI: 10.2210/pdb2h3n/pdb
• Related: 2H32
• Descriptor: VpreB protein, Ig lambda-5 (3 entities in total)
• Functional Keywords: beta sheets, v- and c-type immunoglobulin fold, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted (Potential): P15814
• Total number of polymer chains: 4
• Total formula weight: 48138.13

Authors

Bankovich, A.J.,Garcia, K.C. (deposition date: 2006-05-22, release date: 2007-05-08, Last modification date: 2024-11-06)

Primary citation

Bankovich, A.J.,Raunser, S.,Juo, Z.S.,Walz, T.,Davis, M.M.,Garcia, K.C.
Structural insight into pre-B cell receptor function
Science, 316:291-294, 2007

PubMed Abstract: 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.

PubMed: 17431183
DOI: 10.1126/science.1139412

Experimental method

X-RAY DIFFRACTION (2.3 Å)