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Structural Insight into Pre-B Cell Receptor Function

Science, 13 April 2007
Vol. 316, Issue 5822, p. 291-294
DOI: 10.1126/science.1139412

Structural Insight into Pre-B Cell Receptor Function

  1. Alexander J. Bankovich1,
  2. Stefan Raunser6,
  3. Z. Sean Juo2,3,4,
  4. Thomas Walz6,
  5. Mark M. Davis1,2,5,
  6. K. Christopher Garcia1,2,3,4,*
  1. 1 Program in Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
  2. 2 Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA.
  3. 3 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
  4. 4 Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
  5. 5 Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
  6. 6 Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
  1. * To whom correspondence should be addressed. E-mail: kcgarcia{at}


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 λ5 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.

  • Received for publication 29 December 2006.
  • Accepted for publication 13 March 2007.


A. J. Bankovich, S. Raunser, Z. S. Juo, T. Walz, M. M. Davis, and K. C. Garcia, Structural Insight into Pre-B Cell Receptor Function. Science 316, 291-294 (2007).

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