1iao: Difference between revisions
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[[Image:1iao.gif|left|200px]] | [[Image:1iao.gif|left|200px]] | ||
'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339''' | {{Structure | ||
|PDB= 1iao |SIZE=350|CAPTION= <scene name='initialview01'>1iao</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IAO is a [ | 1IAO 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=1IAO 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: ovalbumin peptide]] | [[Category: ovalbumin peptide]] | ||
''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 11:47:47 2008'' | ||
Revision as of 09:47, 20 March 2008
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| 1iao, resolution 2.6Å | |||||||||||||
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| Ligands: | NAG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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