Binding of an invariant-chain peptide, CLIP, to I-A major histocompatibility complex class II molecules
| Autor: | Anand Gautam, Vanda Quinn, Peter J. Milburn, C.I. Pearson, Hugh O. McDevitt |
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| Rok vydání: | 1995 |
| Předmět: |
CD74
Stereochemistry T-Lymphocytes Antigen presentation Antigen-Presenting Cells Peptide binding Peptide Plasma protein binding Transfection Major histocompatibility complex Cell Line Antigens Neoplasm Animals chemistry.chemical_classification B-Lymphocytes MHC class II Hybridomas Multidisciplinary biology Histocompatibility Antigens Class II Molecular biology Peptide Fragments Recombinant Proteins Antigens Differentiation B-Lymphocyte chemistry Mutagenesis Site-Directed biology.protein Peptides Cell Division Alpha chain Protein Binding Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 92:335-339 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | Invariant chain (Ii) associates with major histocompatibility complex (MHC) class II molecules and is crucial for antigen presentation by class II molecules. The exact nature of Ii interaction with MHC class II molecules remains undefined. A nested set of Ii peptides, CLIPs (class II-associated Ii peptides), have been eluted from various MHC class II molecules, suggesting that CLIPs correspond, at least in part, to the Ii motif which blocks the conventional peptide binding site in MHC class II molecules. Here we report how CLIPs interact with class II MHC molecules, I-A. We have identified regions critical for binding of CLIPs and I-A class II molecules. In most cases, the binding of CLIPs to a number of I-A molecules is modulated by the steric bulk of methionine residues at positions 93 and 99. In addition, the binding of CLIPs to an I-A molecule, I-Au, is sensitive to substitutions at aspartic acid-59 in the alpha chain and threonine-86 in the beta chain, whereas the binding of an antigen-derived peptide is not. Taken together, these results provide an insight as to how CLIPs bind to MHC class II heterodimers. |
| Databáze: | OpenAIRE |
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