Peptide-Major Histocompatibility Complex Class I Complex: From the Structural and Molecular Basis to Pharmacological Principles and Therapeutic Applications View Full Text


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Chapter Info

DATE

1998

AUTHORS

Denis Hudrisier , Jean Edouard Gairin

ABSTRACT

Pathologic states such as viral or parasitic infections, cancer, autoimmune diseases, or graft rejection have in common the development of an immune response that involves the recruitment of activated T cells. T cell activation depends on two fundamental events: (1) the recognition of antigenic peptides associated with major histocompatibility complex (MHC) molecules expressed at the surface of the presenting cells by antigen-specific T cell receptors (TCR) expressed by T cells and (2) the TCR-mediated signal transduction cascade triggered by the association of the TCR with its ligand, the peptide-MHC complex. Peptide-MHC interactions have been studied extensively and are now well understood. Interactions of peptides with MHC class I molecules (recognized by cytotoxic T lymphocytes, CTL) or with MHC class II molecules (recognized by helper T cells) are comparable in some aspects, but differ significantly in others. Their structural and biological principles are well documented (see, e.g., Stern and Wiley 1994; Grey et al. 1995; Madden 1995; Rammensee 1995; Jones 1997 and references cited in these reviews). In the past few years, analysis of the molecular, structural, and biological aspects of MHC-pep- tide-TCR interaction has allowed the pharmacological principles of the interaction between the TCR and its ligand, the peptide-MHC complex, to be established (Hudrisier and Gairin 1996). Indeed, it is now well established that TCR ligands may be endowed with agonist, partial agonist, or antagonist properties (for a review, see, e.g., Jameson and Bevan 1995). More... »

PAGES

75-97

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/978-3-642-72045-1_4

    DOI

    http://dx.doi.org/10.1007/978-3-642-72045-1_4

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9557394


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