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Unusual features of self-peptide/MHC binding by autoimmune T cell receptors Nicholson MJ; Hahn M; Wucherpfennig KWImmunity 2005[Oct]; 23 (4): 351-60Structural studies on T cell receptors (TCRs) specific for foreign antigens demonstrated a remarkably similar topology characterized by a central, diagonal TCR binding mode that maximizes interactions with the MHC bound peptide. However, three recent structures involving autoimmune TCRs demonstrated unusual interactions with self-peptide/MHC complexes. Two TCRs from multiple sclerosis patients bind with unconventional topologies, and both TCRs are shifted toward the peptide N terminus and the MHC class II beta chain helix. A TCR from the experimental autoimmune encephalomyelitis (EAE) model binds in a conventional orientation, but the structure is unusual because the self-peptide only partially fills the binding site. For all three TCRs, interaction with the MHC bound self-peptide is suboptimal, and only two or three TCR loops contact the peptide. Optimal TCR binding modes confer a competitive advantage for antimicrobial T cells during an infection, whereas altered binding properties may permit survival of a subset of autoreactive T cells during thymic selection.|Animals[MESH]|Autoantigens/*chemistry/*immunology/metabolism[MESH]|Autoimmune Diseases/*immunology[MESH]|Complementarity Determining Regions/chemistry/immunology/metabolism[MESH]|Humans[MESH]|Mice[MESH]|Models, Molecular[MESH]|Receptors, Antigen, T-Cell/*chemistry/*immunology/metabolism[MESH] |
