2H32
Crystal structure of the pre-B cell receptor
Summary for 2H32
Entry DOI | 10.2210/pdb2h32/pdb |
Descriptor | Immunoglobulin iota chain, Immunoglobulin omega chain, Immunoglobulin heavy chain, ... (5 entities in total) |
Functional Keywords | beta sheets, v and c-type ig folds, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 3 |
Total formula weight | 52308.18 |
Authors | Bankovich, A.J. (deposition date: 2006-05-22, release date: 2007-04-24, Last modification date: 2023-08-30) |
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 Cited by 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: 17431183DOI: 10.1126/science.1139412 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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