Crystal Structures of Two I-Ad–Peptide Complexes Reveal That High Affinity Can Be Achieved without Large Anchor Residues
Copyright policy )Crystal Structures of Two I-Ad–Peptide Complexes Reveal That High Affinity Can Be Achieved without Large Anchor Residues
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 beta bulge, not seen in I-E and DR structures, that affects numerous interactions between the alpha and beta 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.
- SCRIPPS RESEARCH INSTITUTE
- Scripps Research Institute United States
Models, Molecular, Binding Sites, Ovalbumin, Immunology, Molecular Sequence Data, Histocompatibility Antigens Class II, Models, Immunological, Hemagglutinin Glycoproteins, Influenza Virus, Crystallography, X-Ray, Peptide Fragments, Recombinant Proteins, Mice, Infectious Diseases, Immunology and Allergy, Animals, Dimerization
Models, Molecular, Binding Sites, Ovalbumin, Immunology, Molecular Sequence Data, Histocompatibility Antigens Class II, Models, Immunological, Hemagglutinin Glycoproteins, Influenza Virus, Crystallography, X-Ray, Peptide Fragments, Recombinant Proteins, Mice, Infectious Diseases, Immunology and Allergy, Animals, Dimerization
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