About: Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding     Goto   Sponge   NotDistinct   Permalink

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Description
  • 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...
  • 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... (en)
  • Proteiny hlavního histokompatibilitního systému 2. třídy vážou peptidy a prezentují je na buněčném povrchu, aby mohly reagovat s CD4+ T buňkami jako součást systému, kterým imunitní systém kontroluje příznaky infekce v těle. Na základě různých hydrodynamických a spektroskopických postupů bylo zjištěno, že vazba peptidů vyvolává konformační změny u proteinů MHC 2. třídy, ale tyto změny nebyly v rámci celkové struktury MHC 2. třídy jasně lokalizovány. Abychom zmapovali konformační změnu HLA-DR1, známé varianty MHC 2. třídy, vyvolanou peptidy, připravili jsme sérii monoklonálních protilátek rozpoznávajících podjednotku beta, která je specifická pro prázdnou konformaci. Každá protilátka reagovala s prázdnou formou, ale ne s formou obsazenou peptidem, protože jak rozpustný rekombinantní protein, tak nativní protein byly exprimovány na buněčném povrchu. Epitopy vázající protilátky byly charakterizovány pomocí překrývajících se peptidů a hledání nahrazených alaninů a byly lokalizovány do ... (cs)
Title
  • Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding
  • Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding (en)
  • Monoklonální protilátky specifické pro prázdnou konformaci HLA-DR1 ukazují aspekty konformační změny spojené s vazbou peptidů (cs)
skos:prefLabel
  • Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding
  • Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding (en)
  • Monoklonální protilátky specifické pro prázdnou konformaci HLA-DR1 ukazují aspekty konformační změny spojené s vazbou peptidů (cs)
skos:notation
  • RIV/68378050:_____/04:00105351!RIV/2005/AV0/A23005/N
http://linked.open.../vavai/riv/strany
  • 16561;16570
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LN00A026), Z(AV0Z5052915)
http://linked.open...iv/cisloPeriodika
  • 16
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 574519
http://linked.open...ai/riv/idVysledku
  • RIV/68378050:_____/04:00105351
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • immunoreceptor; signalling (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [EFCBC30A0F6C]
http://linked.open...i/riv/nazevZdroje
  • Journal of Biological Chemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 279
http://linked.open...iv/tvurceVysledku
  • Hořejší, Václav
  • Hilgert, Ivan
  • Strominger, J. L.
  • Palmer, M.
  • Arenas, J. E.
  • Baggio, R. F.
  • Carven, G. J.
  • Chitta, S.
  • Rushe, M. M.
  • Santambrogio, L.
  • Stern, L. J.
http://linked.open...n/vavai/riv/zamer
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