2IAD

CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138

Summary for 2IAD

• Entry DOI: 10.2210/pdb2iad/pdb
• Descriptor: MHC CLASS II I-AD (3 entities in total)
• Functional Keywords: mhc ii, class ii mhc i-ad
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein (Potential): P04228 P01921
• Total number of polymer chains: 2
• Total formula weight: 45708.71

Authors

Scott, C.A.,Peterson, P.A.,Teyton, L.,Wilson, I.A. (deposition date: 1998-03-13, release date: 1998-11-18, Last modification date: 2024-11-20)

Primary citation

Scott, C.A.,Peterson, P.A.,Teyton, L.,Wilson, I.A.
Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues.
Immunity, 8:319-329, 1998

PubMed 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.

PubMed: 9529149
DOI: 10.1016/S1074-7613(00)80537-3

Experimental method

X-RAY DIFFRACTION (2.4 Å)