1iao

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[[Image:1iao.gif|left|200px]]<br /><applet load="1iao" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1iao.gif|left|200px]]
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caption="1iao, resolution 2.6&Aring;" />
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'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339'''<br />
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{{Structure
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|PDB= 1iao |SIZE=350|CAPTION= <scene name='initialview01'>1iao</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1IAO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAO OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9529149 9529149]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:51 2008''
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''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

Image:1iao.gif


PDB ID 1iao

Drag the structure with the mouse to rotate
, resolution 2.6Å
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

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