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Science 13 April 2007:
Vol. 316. no. 5822, pp. 291 - 294
DOI: 10.1126/science.1139412
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Reports

Structural Insight into Pre-B Cell Receptor Function

Alexander J. Bankovich,1 Stefan Raunser,6 Z. Sean Juo,2,3,4 Thomas Walz,6 Mark M. Davis,1,2,5 K. Christopher Garcia1,2,3,4*

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 {lambda}5 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.

1 Program in Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
2 Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA.
3 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
4 Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
5 Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
6 Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

* To whom correspondence should be addressed. E-mail: kcgarcia{at}stanford.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Engineering and characterization of a single chain surrogate light chain variable domain.
L. Morstadt, A. Bohm, D. Yuksel, K. Kumar, B. D. Stollar, and J. D. Baleja (2008)
Protein Sci. 17, 458-465
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Science. ISSN 0036-8075 (print), 1095-9203 (online)