1iao: Difference between revisions

Revision as of 10:40, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1iao.png

Template:STRUCTURE 1iao

CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339

Template:ABSTRACT PUBMED 9529149

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 Tue Jul 1 10:40:36 2008

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OCA

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-'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339'''
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-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9529149}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9529149}}
 ==About this Structure==
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 [[Category: Mhc ii]]
 [[Category: Ovalbumin peptide]]
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