Not just any T cell receptor will do.

Although our structural understanding of T cell recognition has rapidly evolved due to recent crystallographic results, the reality is that detailed answers to many of the most fundamental questions still remain elusive. In this issue, high-resolution insight into the phenomenon of TCR chain bias takes down another brick from the wall.

[1]  Ellis L. Reinherz,et al.  Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[2]  Z Reich,et al.  Ligand recognition by alpha beta T cell receptors. , 1998, Annual review of immunology.

[3]  D. Madden The three-dimensional structure of peptide-MHC complexes. , 1995, Annual review of immunology.

[4]  Brian M. Baker,et al.  αβ T Cell Receptor Ligand-Specific Oligomerization Revisited , 2001 .

[5]  Ian A Wilson,et al.  The specificity of TCR/pMHC interaction. , 2002, Current opinion in immunology.

[6]  D. Stuart,et al.  Crystal structure of the complex between human CD8αα and HLA-A2 , 1997, Nature.

[7]  E. Reinherz,et al.  Mechanisms Contributing to T Cell Receptor Signaling and Assembly Revealed by the Solution Structure of an Ectodomain Fragment of the CD3ϵγ Heterodimer , 2001, Cell.

[8]  Mark M. Davis,et al.  Direct observation of ligand recognition by T cells , 2002, Nature.

[9]  J. Whisstock,et al.  A Structural Basis for the Selection of Dominant αβ T Cell Receptors in Antiviral Immunity , 2003 .

[10]  E. Reinherz,et al.  Involvement of the TCR Cβ FG Loop in Thymic Selection and T Cell Function , 2002, The Journal of experimental medicine.

[11]  T. Schumacher,et al.  Junctional biases in the naive TCR repertoire control the CTL response to an immunodominant determinant of HSV-1. , 2000, Immunity.

[12]  D. Wiley,et al.  T Cell Receptor–MHC Interactions up Close , 2001, Cell.

[13]  J Nikolić-Zugić,et al.  Role of self-peptides in positively selecting the T-cell repertoire. , 1990 .

[14]  Balbino Alarcón,et al.  Recruitment of Nck by CD3ϵ Reveals a Ligand-Induced Conformational Change Essential for T Cell Receptor Signaling and Synapse Formation , 2002, Cell.

[15]  S. Degermann,et al.  T Cell Receptor β Chain Lacking the Large Solvent-exposed Cβ FG Loop Supports Normal α/β T Cell Development and Function in Transgenic Mice , 1999, The Journal of experimental medicine.

[16]  R. Germain Making a molecular match , 1990, Nature.

[17]  Robyn L. Stanfield,et al.  An αβ T Cell Receptor Structure at 2.5 Å and Its Orientation in the TCR-MHC Complex , 1996, Science.

[18]  M. Oldstone Molecular mimicry and autoimmune disease , 1987, Cell.

[19]  Bernard Malissen,et al.  A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. , 2002, Immunity.

[20]  J. McCluskey,et al.  The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance. , 2002, Structure.

[21]  S. Bromley,et al.  The immunological synapse: a molecular machine controlling T cell activation. , 1999, Science.

[22]  D. Wiley,et al.  HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[23]  Mark M. Davis,et al.  Two-step binding mechanism for T-cell receptor recognition of peptide–MHC , 2002, Nature.