Crystal structure of a T cell receptor bound to an allogeneic MHC molecule - PubMed (original) (raw)
Crystal structure of a T cell receptor bound to an allogeneic MHC molecule
J B Reiser et al. Nat Immunol. 2000 Oct.
Erratum in
- Nat Immunol 2000 Nov;1(5):447
Abstract
Many T cell receptors (TCRs) that are selected to respond to foreign peptide antigens bound to self major histocompatibility complex (MHC) molecules are also reactive with allelic variants of self-MHC molecules. This property, termed alloreactivity, causes graft rejection and graft-versus-host disease. The structural features of alloreactivity have yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC class I molecule. A distinguishing feature of this complex is that the eleven-residue-long complementarity-determining region 3 (CDR3) found in the BM3.3 TCR alpha chain folds away from the peptide binding groove and makes no contact with the bound peptide, the latter being exclusively contacted by the BM3.3 CDR3 beta. Our results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-MHC molecules.
Comment in
- Incompatible differences: view of an allogeneic pMHC-TCR complex.
Kranz DM. Kranz DM. Nat Immunol. 2000 Oct;1(4):277-8. doi: 10.1038/79716. Nat Immunol. 2000. PMID: 11017095 No abstract available.
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