Accueil > Publications > Recherche par années > Années 2000 > 2007

Mazza, C ; Auphan-Anezin, N ; Gregoire, C ; Guimezanes, A ; Kellenberger, C ; Roussel, A ; Kearney, A ; van der Merwe, PA ; Schmitt-Verhulst, AM ; Malissen, B

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides ?

Embo Journal 26 (7) 1972-1983

par Administrateur - publié le

Abstract :

Binding degeneracy is thought to constitute a fundamental property of the T-cell antigen receptor (TCR), yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and a peptide (pBM8) bound to the H-2K(bm8) major histocompatibility complex (MHC) molecule, and compared it with the structures of the BM3.3 TCR bound to H-2K(b) molecules loaded with two peptides that had a minimal level of primary sequence identity with pBM8. Our findings provide a refined structural view of the basis of BM3.3 TCR cross-reactivity and a structural explanation for the long-standing paradox that a TCR antigen-binding site can be both specific and degenerate.