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Immunity. 1998 Mar;8(3):319-29.

Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues.

Author information

1
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

Erratum in

  • Immunity 1998 Apr;8(4):531.

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 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.

PMID:
9529149
DOI:
10.1016/s1074-7613(00)80537-3
[Indexed for MEDLINE]
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