The TCR is an allosterically regulated macromolecular machinery changing its conformation while working

Immunol Rev.                  online article

In our Excellence Cluster projects we study the mechanisms with which the αβ T cell receptor (TCR) is activated by ligand binding. The TCR is a multiprotein complex controlling the development, differentiation and activation of T cells. Although the structure of the complete TCR is not known, cumulative evidence supports that the TCR cycles between different conformational states. These structural transitions determine whether the TCR engages intracellular effectors or not, regulating TCR phosphorylation and signaling. As for other membrane receptors, ligand binding selects and stabilizes the TCR in active conformations, and/or switches the TCR to activating states that were not visited before ligand engagement. In this extensive review Schamel and Minguet discuss the main models of TCR allostery, that is, how ligand binding at the ectodomains changes the structure at the cytoplasmic tails.