Journal
IMMUNITY
Volume 14, Issue 1, Pages 81-92Publisher
CELL PRESS
DOI: 10.1016/S1074-7613(01)00091-7
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Funding
- NCI NIH HHS [CA58896] Funding Source: Medline
- NIMH NIH HHS [MH19185] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA058896] Funding Source: NIH RePORTER
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The rat MHC class la molecule RT1-A(a) 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-A(a)-MTF-E at 2.55 Angstrom 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.
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