2h32 | pdb_00002h32
Crystal structure of the pre-B cell receptor
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[VPREB_HUMAN] Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation. [IGLL1_HUMAN] Critical for B-cell development.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structural insight into pre-B cell receptor function.,Bankovich AJ, Raunser S, Juo ZS, Walz T, Davis MM, Garcia KC Science. 2007 Apr 13;316(5822):291-4. PMID:17431183[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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