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1iao

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(New page: 200px<br /><applet load="1iao" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iao, resolution 2.6&Aring;" /> '''CLASS II MHC I-AD IN ...)
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[[Image:1iao.gif|left|200px]]<br /><applet load="1iao" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1iao.gif|left|200px]]<br /><applet load="1iao" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1iao, resolution 2.6&Aring;" />
caption="1iao, resolution 2.6&Aring;" />
'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339'''<br />
'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339'''<br />
==Overview==
==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.
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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.
==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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAO OCA].
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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].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Peterson, P.A.]]
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[[Category: Peterson, P A.]]
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[[Category: Scott, C.A.]]
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[[Category: Scott, C A.]]
[[Category: Teyton, L.]]
[[Category: Teyton, L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: class ii mhc]]
[[Category: class ii mhc]]
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[[Category: ovalbumin peptide]]
[[Category: ovalbumin peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:13:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:51 2008''

Revision as of 11:09, 21 February 2008


1iao, resolution 2.6Å

Drag the structure with the mouse to rotate

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 with as ligand. 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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