[HTML][HTML] Alloreactivity between disparate cognate and allogeneic pMHC-I complexes is the result of highly focused, peptide-dependent structural mimicry
Our understanding of the molecular mechanisms of T cell alloreactivity remains limited by
the lack of systems for which both the T cell receptor allo-and cognate ligand are known.
Here we provide evidence that a single alloreactive T cell receptor interacts with analogous
structural regions of its cognate ligand, HLA-B* 0801 FLRGRAYGL, as its allogeneic ligand,
HLA-B* 3501 KPIVVLHGY. The crystal structures of the binary peptide-major
histocompatibility complexes show marked differences in the conformation of the heavy …
the lack of systems for which both the T cell receptor allo-and cognate ligand are known.
Here we provide evidence that a single alloreactive T cell receptor interacts with analogous
structural regions of its cognate ligand, HLA-B* 0801 FLRGRAYGL, as its allogeneic ligand,
HLA-B* 3501 KPIVVLHGY. The crystal structures of the binary peptide-major
histocompatibility complexes show marked differences in the conformation of the heavy …