1iao
From Proteopedia
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CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339
Overview
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.
About this Structure
1IAO is a Protein complex structure of sequences from Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues., Scott CA, Peterson PA, Teyton L, Wilson IA, Immunity. 1998 Mar;8(3):319-29. PMID:9529149
Page seeded by OCA on Tue Nov 20 17:13:21 2007
Categories: Mus musculus | Protein complex | Peterson, P.A. | Scott, C.A. | Teyton, L. | Wilson, I.A. | NAG | Class ii mhc | I-a | Mhc ii | Ovalbumin peptide
