![]() ![]() Second, I show that the proposed “scoop loop” of TAPBPR is unimportant for chaperoning ability and show that the important regions of TAPBPR for this activity are located where the protein interacts with the base of the MHC-I α2 helix as Ill as beta-2-microglobulin. Additionally, there is a folded protein motif within the α2 helix of the MHC-I that TAPBPR is recognizing to bind as a chaperone. First, I show that TAPBPR can bind as a chaperone with broad MHC-I allelic recognition but has narrow MHC-I specificity in regard to peptide editing. Here, using biochemical and biophysical assays, I characterize the mechanism of TAPBPR, a chaperone and peptide editor that is independent of the peptide loading complex. ![]() The mechanism of peptide loading, termed antigen presentation, by chaperones, tapasin and TAPBPR, is unclear. Peptides from non-self proteins can be recognized by surveilling T cells leading to cell lysis. Degree Level Dissertation Keyword(s) immunology, protein Abstract Class I major histocompatibility complexes (MHC-I) play an important role in the adaptive immune system as they present peptides on the cell surface. Title Investigating the molecular mechanisms of chaperones involved in antigen presentation Author(s) Devlin, Christine Anne Date of Publication Director of Research (if dissertation) or Advisor (if thesis) Procko, Erik Doctoral Committee Chair(s) Procko, Erik Committee Member(s)ĭepartment of Study Biochemistry Discipline Biochemistry Degree Granting Institution University of Illinois at Urbana-Champaign Degree Name Ph.D. This item's files can only be accessed by the Administrator group. ![]()
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