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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa.

The rat MHC class Ia molecule RT1-Aa has the unusual capacity to bind long peptides ending in arginine, such as MTF-E, a thirteen-residue, maternally transmitted minor histocompatibility antigen. The antigenic structure of MTF-E was unpredictable due to its extraordinary length and two arginines that could serve as potential anchor residues. The crystal structure of RT1-Aa-MTF-E at 2.55 A shows that both peptide termini are anchored, as in other class I molecules, but the central residues in two independent pMHC complexes adopt completely different bulged conformations based on local environment. The MTF-E epitope is fully exposed within the putative T cell receptor (TCR) footprint. The flexibility demonstrated by the MTF-E structures illustrates how different TCRs may be raised against chemically identical, but structurally dissimilar, pMHC complexes.[1]

References

  1. Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa. Speir, J.A., Stevens, J., Joly, E., Butcher, G.W., Wilson, I.A. Immunity (2001) [Pubmed]
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