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  • Title: Recognition of altered self major histocompatibility complex molecules modulated by specific peptide interactions.
    Author: Nepom GT, Ou D, Lybrand TP, DeWeese C, Domeier ME, Buckner JH, Mitchell LA, Tingle AJ.
    Journal: Eur J Immunol; 1996 Apr; 26(4):949-52. PubMed ID: 8625994.
    Abstract:
    Antigen-specific and major histocompatibility complex (MHC)-restricted recognition by the T cell receptor involves multiple structural contacts over a large molecular surface area. Using a human T cell clone specific for a rubella viral peptide restricted by subsets of HLA DR4 molecules, we identified structurally diverse combinations of peptide-MHC complexes which were functionally equivalent to T cell recognition. Presentation of the rubella-derived peptide on DR4 molecules with an E-74 polymorphism triggered T cell recognition, as did presentation of a single amino acid-substituted peptide in the context of DR4 molecule which lacked the E-74 site. Peptide binding and molecular modeling analysis indicates the structural and functional complementarity of T cell recognition for a specific amino acid side chain, whether contributed by the peptide or by the MHC molecule.
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