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1iao
From Proteopedia
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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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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| 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
Page seeded by OCA on Thu Mar 20 11:47:47 2008
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
