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- W2028663182 abstract "We have determined the structures of I-Ad covalently linked to an ovalbumin peptide (OVA323–339) and to an influenza virus hemagglutinin peptide (HA126–138). The floor of the peptide-binding groove contains an unusual β bulge, not seen in I-E and DR structures, that affects numerous interactions between the α and β chains and bound peptide. Unlike other MHC–peptide complexes, the peptides do not insert any large anchor residues into the binding pockets of the shallow I-Ad binding groove. The previously identified six-residue “core” binding motif of I-Ad occupies only the P4 to P9 pockets, implying that specificity of T cell receptor recognition of I-Ad–peptide complexes can be accomplished by peptides that only partially fill the MHC groove." @default.
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- W2028663182 date "1998-03-01" @default.
- W2028663182 modified "2023-10-16" @default.
- W2028663182 title "Crystal Structures of Two I-Ad–Peptide Complexes Reveal That High Affinity Can Be Achieved without Large Anchor Residues" @default.
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- W2028663182 doi "https://doi.org/10.1016/s1074-7613(00)80537-3" @default.
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