Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function
Author:
Funder
Cancer Research UK Program
BBSRC Project
Publisher
Elsevier BV
Subject
Molecular Biology,Immunology
Reference22 articles.
1. Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/beta 2m heterodimer;Bouvier;Nat. Struct. Biol.,1998
2. Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection;Chen;EMBO J.,2007
3. Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer;Dong;Immunity,2009
4. Competition for access to the rat major histocompatibility complex class I peptide-loading complex reveals optimization of peptide cargo in the absence of transporter associated with antigen processing (TAP) association;Ford;J. Biol. Chem.,2004
5. Impaired immune responses and altered peptide repertoire in tapasin-deficient mice;Garbi;Nat. Immunol.,2000
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3. Tapasin-mediated editing of the MHC I immunopeptidome is epitope specific and dependent on peptide off-rate, abundance, and level of tapasin expression;Frontiers in Immunology;2022-10-31
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