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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}stanford.edu

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 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.

Citation:

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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L. Elantak, M. Espeli, A. Boned, O. Bornet, J. Bonzi, L. Gauthier, M. Feracci, P. Roche, F. Guerlesquin, C. Schiff et al.
J Biol Chem 287, 44703-44713 (28 December 2012)

The Non-Ig Parts of the VpreB and {lambda}5 Proteins of the Surrogate Light Chain Play Opposite Roles in the Surface Representation of the Precursor B Cell Receptor
M. Knoll, Y. Yanagisawa, S. Simmons, N. Engels, J. Wienands, F. Melchers, and K. Ohnishi
J. Immunol. 188, 6010-6017 (15 June 2012)

Core Fucosylation of {mu} Heavy Chains Regulates Assembly and Intracellular Signaling of Precursor B Cell Receptors
W. Li, Q. Liu, Y. Pang, J. Jin, H. Wang, H. Cao, Z. Li, X. Wang, B. Ma, Y. Chi et al.
J Biol Chem 287, 2500-2508 (20 January 2012)

Mechanism for Pre-B Cell Loss in VH-Mutant Rabbits
G. R. Robbins, and K. L. Knight
J. Immunol. 187, 4714-4720 (1 November 2011)

Selection of Individual VH Genes Occurs at the Pro-B to Pre-B Cell Transition
W. Meng, L. Yunk, L.-S. Wang, A. Maganty, E. Xue, P. L. Cohen, R. A. Eisenberg, M. G. Weigert, S. J. C. Mancini, E. T. Luning Prak et al.
J. Immunol. 187, 1835-1844 (15 August 2011)

B-cell receptors and heavy chain diseases: guilty by association?
D. Corcos, M. J. Osborn, and L. S. Matheson
Blood 117, 6991-6998 (30 June 2011)

Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-{beta} binding
S. J. Lin, Y. Hu, J. Zhu, T. K. Woodruff, and T. S. Jardetzky
Proc. Natl. Acad. Sci. USA 108, 5232-5236 (29 March 2011)

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S. Minguet, E.-P. Dopfer, and W. W. A. Schamel
Int Immunol 22, 205-212 (1 March 2010)

Immunoglobulin aggregation leading to Russell body formation is prevented by the antibody light chain
D. Corcos, M. J. Osborn, L. S. Matheson, F. Santos, X. Zou, J. A. Smith, G. Morgan, A. Hutchings, M. Hamon, D. Oxley et al.
Blood 115, 282-288 (14 January 2010)

Pathogenesis, Diagnosis, and Management of Primary Antibody Deficiencies and Infections
A. J. Fried, and F. A. Bonilla
Clin. Microbiol. Rev. 22, 396-414 (1 July 2009)

PKC{eta} directs induction of IRF-4 expression and Ig {kappa} gene rearrangement in pre-BCR signaling pathway
A. Oda, T. Ono, M. Yamamoto, R. Goitsuka, and D. Kitamura
Int Immunol 20, 1417-1426 (1 November 2008)

A Unique Role for the {lambda}5 Nonimmunoglobulin Tail in Early B Lymphocyte Development
C. Vettermann, K. Herrmann, C. Albert, E. Roth, M. R. Bosl, and H.-M. Jack
J. Immunol. 181, 3232-3242 (1 September 2008)

B lymphocytes: how they develop and function
T. W. LeBien, and T. F. Tedder
Blood 112, 1570-1580 (1 September 2008)

Combinatorial surrobody libraries
L. Xu, H. Yee, C. Chan, A. K. Kashyap, L. Horowitz, M. Horowitz, R. R. Bhatt, and R. A. Lerner
Proc. Natl. Acad. Sci. USA 105, 10756-10761 (5 August 2008)

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