1iao: Difference between revisions
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'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339''' | '''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339''' | ||
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[[Category: Teyton, L.]] | [[Category: Teyton, L.]] | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
[[Category: | [[Category: Class ii mhc]] | ||
[[Category: | [[Category: I-a]] | ||
[[Category: | [[Category: Mhc ii]] | ||
[[Category: | [[Category: Ovalbumin peptide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:46:43 2008'' | |||
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Revision as of 19:46, 2 May 2008
CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339
OverviewOverview
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 StructureAbout this Structure
1IAO is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 19:46:43 2008