title: Biophysical and structural studies of TCRs and ligands: implications for T cell signaling.
abstract: The availability of soluble alphabeta TCRs and the individual chains has now made it possible to carry out structural studies of these molecules and analyze their molecular interactions with peptide-MHC ligands. Recent X-ray crystallographic structures of TCR alpha and beta chains have finally established their structural similarity with the lg molecules. Kinetic measurements of the interaction between TCRs and their ligands have provided strong evidence in favour of an affinity/avidity model for T cell activation in the periphery as well as during development in the thymus.
authors.affiliation: Cancer Immunobiology Center, Department of Microbiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235-8576, USA. Sally@skylab.swmed.edu
authors.forename: E S
authors.initials: ES
authors.lastname: Ward
authors.forename: A
authors.initials: A
authors.lastname: Qadri
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D006801:Humans; D016693:Receptors, Antigen, T-Cell, alpha-beta / Q000737:chemistry* / Q000502:physiology*; D015398:Signal Transduction / Q000276:immunology*; D013329:Structure-Activity Relationship; D013601:T-Lymphocytes / Q000737:chemistry* / Q000378:metabolism
chemical_list: D016693:Receptors, Antigen, T-Cell, alpha-beta