The engagement of the T cell receptor (TCR) to its ligand, the major histoc
ompatibility complex (MHC)-peptide complex, leads to T cell activation. The
molecular mechanisms leading to this activation are still unknown. Dimeriz
ation or substantial conformational changes following TCR ligation have not
been observed by classical biochemical methods or by X-ray crystallography
of the TCR/MHC complex. However, most of these experiments have used reduc
tionist approaches in which only MHC and TCR molecules were taken into acco
unt. In fact, the TCR is only one of many molecules forming the TCR complex
(TCRC), and the interplay among the components of this larger complex have
not been studied in depth. The reconstitution of a complete TCRC using rec
ombinant molecules is our goal and will be the first step to new structural
and functional studies.