TAPBPR uses the same residues as tapasin to associate with MHC class I
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چکیده
منابع مشابه
The binding of TAPBPR and Tapasin to MHC class I is mutually exclusive.
The loading of peptide Ags onto MHC class I molecules is a highly controlled process in which the MHC class I-dedicated chaperone tapasin is a key player. We recently identified a tapasin-related molecule, TAPBPR, as an additional component in the MHC class I Ag-presentation pathway. In this study, we show that the amino acid residues important for tapasin to interact with MHC class I are highl...
متن کاملTAPBPR isoforms exhibit altered association with MHC class I
The tapasin-related protein TAPBPR is a novel component of the antigen processing and presentation pathway, which binds to MHC class I coupled with β2-microglobulin. We describe six alternatively spliced TAPBPR transcripts from the TAPBPL gene and investigate three of these at a protein level. TAPBPR transcripts lacking exon 5 result in loss of the membrane proximal IgC domain and loss of abili...
متن کاملInteraction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing.
Peptide loading of major histocompatibility complex class I (MHC-I) molecules is central to antigen presentation, self-tolerance, and CD8(+) T-cell activation. TAP binding protein, related (TAPBPR), a widely expressed tapasin homolog, is not part of the classical MHC-I peptide-loading complex (PLC). Using recombinant MHC-I molecules, we show that TAPBPR binds HLA-A*02:01 and several other MHC-I...
متن کاملTAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst
Our understanding of the antigen presentation pathway has recently been enhanced with the identification that the tapasin-related protein TAPBPR is a second major histocompatibility complex (MHC) class I-specific chaperone. We sought to determine whether, like tapasin, TAPBPR can also influence MHC class I peptide selection by functioning as a peptide exchange catalyst. We show that TAPBPR can ...
متن کاملTapasin shapes immunodominance hierarchies according to the kinetic stability of peptide-MHC class I complexes.
Peptide loading of MHC class I molecules involves multiple cofactors including tapasin. We showed previously in vitro that tapasin edits the peptide repertoire by favoring the binding of peptides with slow dissociation rates. Here, using tapasin-deficient mice and a DNA vaccine that primes directly, we confirm that tapasin establishes hierarchical responses in vivo according to peptide-MHC stab...
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ژورنال
عنوان ژورنال: Frontiers in Immunology
سال: 2013
ISSN: 1664-3224
DOI: 10.3389/conf.fimmu.2013.02.01042