Writing in an August 18 article in the journal Cell, the authors noted that comparisons of the ligand-bound and unliganded receptors -- along with molecular dynamics simulations -- indicate that T-cell receptors can be triggered in the absence of spontaneous structural rearrangements.

The researchers contend that the cryo-EM structure of the fully assembled TCR complex with a tumor-associated peptide/major histocompatibility complex (MHC) ligand provides important insights into the biology of TCR signaling, helping to understand a fundamental process which may pave the way for novel therapeutic approaches targeting severe diseases.

"Our structure is a blueprint for future studies on T-cell activation," Robert Tampé, PhD, director of the Institute of Biochemistry at Goethe University Frankfurt, said in a statement. "In addition, it's an important stimulus for employing the T-cell receptor in a therapeutic context for treating infections, cancer, and autoimmune diseases."

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