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Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding
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SYSNO ASEP 0105351 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding Title Monoklonální protilátky specifické pro prázdnou konformaci HLA-DR1 ukazují aspekty konformační změny spojené s vazbou peptidů Author(s) Carven, G. J. (US)
Chitta, S. (US)
Hilgert, Ivan (UMG-J)
Rushe, M. M. (US)
Baggio, R. F. (US)
Palmer, M. (US)
Arenas, J. E. (US)
Strominger, J. L. (US)
Hořejší, Václav (UMG-J) RID
Santambrogio, L. (US)
Stern, L. J. (US)Source Title Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
Roč. 279, č. 16 (2004), s. 16561-16570Number of pages 9 s. Language eng - English Country US - United States Keywords immunoreceptor ; signalling Subject RIV EC - Immunology R&D Projects LN00A026 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z5052915 - UMG-J Annotation Class II major histocompatibility complex (MHC) proteins bind peptides and present them at the cell surface for interaction with CD4+ T cells as part of the system by which the immune system surveys the body for signs of infection. Peptide binding is known to induce conformational changes in class II MHC proteins on the basis of a variety of hydrodynamic and spectroscopic approaches, but the changes have not been clearly localized within the overall class II MHC structure. To map the peptide-induced conformational change for HLA-DR1, a common human class II MHC variant, we generated a series of monoclonal antibodies recognizing the beta subunit that are specific for the empty conformation. Each antibody reacted with the empty but not the peptide-loaded form, for both soluble recombinant protein and native protein expressed at the cell surface. Antibody binding epitopes were characterized using overlapping peptides and alanine scanning substitutions and were localized to two distinct regions of the protein. The pattern of key residues within the epitopes suggested that the two epitope regions undergo substantial conformational alteration during peptide binding. These results illuminate aspects of the structure of the empty forms and the nature of the peptide-induced conformational change Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2005
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