1iak: Difference between revisions

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New page: left|200px<br /><applet load="1iak" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iak, resolution 1.9Å" /> '''HISTOCOMPATIBILITY AN...
 
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[[Image:1iak.gif|left|200px]]<br /><applet load="1iak" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1iak.gif|left|200px]]<br /><applet load="1iak" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1iak, resolution 1.9&Aring;" />
caption="1iak, resolution 1.9&Aring;" />
'''HISTOCOMPATIBILITY ANTIGEN I-AK'''<br />
'''HISTOCOMPATIBILITY ANTIGEN I-AK'''<br />


==Overview==
==Overview==
We have determined the structure of murine MHC class II I-Ak in complex, with a naturally processed peptide from hen egg lysozyme (HEL residues, 50-62) at 1.9 A resolution. These results provide a structural basis for, the I-Ak peptide-binding motif. Binding is established by the deep burial, of five anchor side chains into specific pockets of the I-Ak binding, groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also, show that in the I-Ak alpha chain, a bulge occurs in the first strand of, the peptide-binding platform, an insertion probably common to all I-A and, HLA-DQ alleles. The I-Ak beta chain has a deletion in the helical region, adjacent to the P7 pocket and an insertion in the helical region, neighboring the P1 pocket. As a result of these structural features, the, extended HEL peptide dips low into the center of the I-Ak groove and, reaches toward solvent at its C-terminal end.
We have determined the structure of murine MHC class II I-Ak in complex with a naturally processed peptide from hen egg lysozyme (HEL residues 50-62) at 1.9 A resolution. These results provide a structural basis for the I-Ak peptide-binding motif. Binding is established by the deep burial of five anchor side chains into specific pockets of the I-Ak binding groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also show that in the I-Ak alpha chain, a bulge occurs in the first strand of the peptide-binding platform, an insertion probably common to all I-A and HLA-DQ alleles. The I-Ak beta chain has a deletion in the helical region adjacent to the P7 pocket and an insertion in the helical region neighboring the P1 pocket. As a result of these structural features, the extended HEL peptide dips low into the center of the I-Ak groove and reaches toward solvent at its C-terminal end.


==About this Structure==
==About this Structure==
1IAK 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=1IAK OCA].  
1IAK 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=1IAK OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Fremont, D.H.]]
[[Category: Fremont, D H.]]
[[Category: Hendrickson, W.A.]]
[[Category: Hendrickson, W A.]]
[[Category: Unanue, E.R.]]
[[Category: Unanue, E R.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: histocompatibility antigen]]
[[Category: histocompatibility antigen]]
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[[Category: peptide complex]]
[[Category: peptide complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:13:16 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:43 2008''

Revision as of 14:09, 21 February 2008

File:1iak.gif


1iak, resolution 1.9Å

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HISTOCOMPATIBILITY ANTIGEN I-AK

OverviewOverview

We have determined the structure of murine MHC class II I-Ak in complex with a naturally processed peptide from hen egg lysozyme (HEL residues 50-62) at 1.9 A resolution. These results provide a structural basis for the I-Ak peptide-binding motif. Binding is established by the deep burial of five anchor side chains into specific pockets of the I-Ak binding groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also show that in the I-Ak alpha chain, a bulge occurs in the first strand of the peptide-binding platform, an insertion probably common to all I-A and HLA-DQ alleles. The I-Ak beta chain has a deletion in the helical region adjacent to the P7 pocket and an insertion in the helical region neighboring the P1 pocket. As a result of these structural features, the extended HEL peptide dips low into the center of the I-Ak groove and reaches toward solvent at its C-terminal end.

About this StructureAbout this Structure

1IAK is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of I-Ak in complex with a dominant epitope of lysozyme., Fremont DH, Monnaie D, Nelson CA, Hendrickson WA, Unanue ER, Immunity. 1998 Mar;8(3):305-17. PMID:9529148

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