2iad: Difference between revisions
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[[Image:2iad.gif|left|200px]] | [[Image:2iad.gif|left|200px]] | ||
'''CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138''' | {{Structure | ||
|PDB= 2iad |SIZE=350|CAPTION= <scene name='initialview01'>2iad</scene>, resolution 2.4Å | |||
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'''CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2IAD is a [ | 2IAD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IAD OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9529149 9529149] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: mhc ii]] | [[Category: mhc ii]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:10 2008'' | ||
Revision as of 15:27, 20 March 2008
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CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138
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
2IAD is a Protein complex structure of sequences from Mus musculus. 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
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