1iak
From Proteopedia
(New page: 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=" | + | [[Image:1iak.gif|left|200px]]<br /><applet load="1iak" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iak, resolution 1.9Å" /> | caption="1iak, resolution 1.9Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Fremont, D H.]] |
| - | [[Category: Hendrickson, W | + | [[Category: Hendrickson, W A.]] |
| - | [[Category: Unanue, E | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:43 2008'' |
Revision as of 11:09, 21 February 2008
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HISTOCOMPATIBILITY ANTIGEN I-AK
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.
About this Structure
1IAK is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:09:43 2008
