1iak
From Proteopedia
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| - | [[Image:1iak.gif|left|200px]] | + | [[Image:1iak.gif|left|200px]] |
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| - | '''HISTOCOMPATIBILITY ANTIGEN I-AK''' | + | {{Structure |
| + | |PDB= 1iak |SIZE=350|CAPTION= <scene name='initialview01'>1iak</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HISTOCOMPATIBILITY ANTIGEN I-AK''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IAK is a [ | + | 1IAK 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=1IAK OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9529148 9529148] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptide complex]] | [[Category: peptide complex]] | ||
| - | ''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 11:47:46 2008'' |
Revision as of 09:47, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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