Peptide Binding to Active Class II MHC Protein on the Cell Surface
| Autor: | Harden M. McConnell, Judith F. Vacchino |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
T cell
Molecular Sequence Data Immunology Cytochrome c Group Peptide Peptide binding CHO Cells Moths Transfection Major histocompatibility complex Mice Cricetinae Extracellular medicine Animals Immunology and Allergy Biotinylation Amino Acid Sequence Sodium Azide chemistry.chemical_classification Antigen Presentation Brefeldin A biology Chinese hamster ovary cell Cell Membrane Histocompatibility Antigens Class II Chloroquine MHC restriction Peptide Fragments Kinetics Protein Transport medicine.anatomical_structure Solubility chemistry Biochemistry biology.protein Intracellular Protein Binding |
| Zdroj: | The Journal of Immunology. 166:6680-6685 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.166.11.6680 |
| Popis: | Solution studies have demonstrated the existence of two functionally distinct isomers of empty class II MHC: an active isomer that binds peptide and an inactive isomer that does not. Empty MHC molecules on the surface of APCs can load antigenic peptides directly from the extracellular medium, facilitating the generation of a diverse peptide repertoire for T cell presentation. In this report, we examine I-Ek on the surface of Chinese hamster ovary cells with respect to the active and inactive isomers. As in the case of purified soluble active I-Ek, active I-Ek on the cell surface is unstable, decaying to the inactive form in ∼14 min. Evidence is presented suggesting that at steady state |
| Databáze: | OpenAIRE |
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