Structural mutations in the constant region of the T-cell antigen receptor (TCR)beta chain and their effect on TCR alpha and beta chain interaction.

The region responsible for T-cell receptor (TCR)alpha and beta chain assembly has previously been shown to reside in their extracellular domains. In an attempt to delineate further the structural requirements for TCR alpha and beta chain assembly, chimeric TCR beta chains with increasing length of constant (C) region and mutant TCR beta chains with C-domain point mutations were constructed. Their ability to assemble with wild-type TCR alpha chain was evaluated in non-T (COS cells) or T cells. The results reveal that the C beta domain is the binding region to TCR alpha chain, whereas the intact variable (V), diversity (D) and joining (J) regions with a short C-domain of beta chain are not sufficient for the TCR alpha and beta chain assembly. The unique interchain disulphide bond between TCR alpha and beta chains is not required for the TCR alpha beta heterodimer formation.