An evolutionary and structural perspective on T cell antigen receptor function.
After a brief overview of the themes and variations that occur in the family of receptors containing immunoreceptor tyrosine-based activation motifs (ITAMs), and of recent structural data on the ligand-binding subunits of these receptors, we use these data to revisit how information on the state and quality of occupancy of the binding site of the T cell antigen receptor (TCR) is conveyed to the proximal components of the TCR transduction cassette.
Malissen
Bernard
B
Centre d'Immunologie INSERM-CNRS de Marseille-Luminy, Marseille, France. bernardm@ciml.univ-mrs.fr
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D017252:CD3 Complex / Q000502:physiology; D015704:CD4 Antigens / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D011505:Protein-Tyrosine Kinases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D016415:Sequence Alignment; D015398:Signal Transduction / Q000502:physiology; D014443:Tyrosine / Q000502:physiology
D017252:CD3 Complex; D015704:CD4 Antigens; C067361:CD8 receptor; D011948:Receptors, Antigen, T-Cell; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases