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|標題:||Complex formation between the lumenal domain of adenovirus E3-19k protein and the extracellular domain of class I MHC molecule in vitro||作者:||Liao, P.H.
|關鍵字:||complex formation;adenovirus E3-19k protein;major histocompatibility;complex (MHC);HLA-A*0201;nf-kappa-b;e3/19k protein;escherichia-coli;antigen;binding;type-2;association;activation;epitope;pathway||Project:||Journal of the Chinese Chemical Society||期刊/報告no：:||Journal of the Chinese Chemical Society, Volume 49, Issue 4, Page(s) 607-610.||摘要:||
The Ad2 E3-19k protein inhibits the transport of newly synthesized class I MHC molecules to the cell surface, thereby interfering with antigen presentation. The detai Is of the interaction between E3-19k protein and class I MHC molecules have not been well-defined. In this present study, we describe the use of gel filtration HPLC for confirming the binding interaction of two domain proteins, E3-19k and MHC class I antigen, and subsequently the characterization of protein complex by SDS-PAGE. Our results demonstrate the complex formation between Ad2 lumenal E3-19k (108 amino acids, wt 108) and HLA-A*0201 molecule in vitro. Titration experiments will be employed in the future to determine stoichiometry and verify the specific interactions.
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