Crystal Structure of I-Ak in Complex with a Dominant Epitope of Lysozyme
| Autor: | Wayne A. Hendrickson, Christopher A. Nelson, Didier Monnaie, Daved H. Fremont, Emil R. Unanue |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Protein Conformation Molecular Sequence Data Immunology Peptide Crystal structure Biology Crystallography X-Ray Protein Structure Secondary Epitope Mice chemistry.chemical_compound Hen Egg Lysozyme Aspartic acid Side chain Animals Immunology and Allergy Amino Acid Sequence Genetics chemistry.chemical_classification Antigen Presentation Binding Sites Sequence Homology Amino Acid Immunodominant Epitopes HLA-DR1 Antigen Histocompatibility Antigens Class II Models Immunological Hydrogen Bonding Peptide Fragments Recombinant Proteins Crystallography Infectious Diseases chemistry Muramidase Lysozyme |
| Zdroj: | Immunity. 8:305-317 |
| ISSN: | 1074-7613 |
| DOI: | 10.1016/s1074-7613(00)80536-1 |
| Popis: | We have determined the structure of murine MHC class II I-A k 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-A k peptide-binding motif. Binding is established by the deep burial of five anchor side chains into specific pockets of the I-A k binding groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also show that in the I-A k α 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-A k β 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-A k groove and reaches toward solvent at its C-terminal end. |
| Databáze: | OpenAIRE |
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