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The Hy.1B11 TCR recognizes the MBP (85-99) peptide bound in the same register to DQ1. This TCR has a higher affinity for its pMHC target than the previously crystallized self-reactive TCRs Ob.1A12 and 3A6. However, the Hy.1B11 TCR is HLA-DQ restricted, whereas the other two TCRs are HLA-DR restricted. HLA-DQ molecules are expressed at ∼10-fold lower levels than HLA-DR molecules, and the higher affinity of Hy.1B11 TCR may therefore be required for this TCR to adequately respond to the self-peptide on peripheral antigen-presenting cells. HLA-DQ molecules are expressed at very low levels in the medulla of the thymus, which may have facilitated escape of negative selection by the Hy.1B11 T cell. It is also possible that the tilted binding mode of Hy.1B11 TCR binding affects formation of higher order structures among TCRs and/or other proteins involved in T cell activation at the immunological synapse.
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