title: Biophysical studies of T-cell receptors and their ligands.
abstract: Recently developed methodologies for the production of the soluble extracellular domains of alpha beta TCRs have allowed several biophysical characterizations. The thermodynamic and kinetic parameters associated with specific ligand interactions between the TCR and MHC-peptide complexes, as well as superantigens, are now being established. Crystallographic studies of isolated TCR fragments have yielded the structures of a V alpha domain and the two extracellular domains of a beta-chain. These investigations are beginning to allow a new visualization of antigen recognition and T-cell activation processes.
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. fremont@columbia.edu
authors.forename: D H
authors.initials: DH
authors.lastname: Fremont
authors.forename: W A
authors.initials: WA
authors.lastname: Rees
authors.forename: H
authors.initials: H
authors.lastname: Kozono
mesh_terms: D000818:Animals; D003460:Crystallization; D006649:Histocompatibility Antigens / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D017260:Receptor-CD3 Complex, Antigen, T-Cell / Q000737:chemistry; D016693:Receptors, Antigen, T-Cell, alpha-beta / Q000737:chemistry*; D016692:Receptors, Antigen, T-Cell, gamma-delta / Q000737:chemistry; D011994:Recombinant Proteins / Q000378:metabolism; D013601:T-Lymphocytes / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D006649:Histocompatibility Antigens; D008024:Ligands; D017260:Receptor-CD3 Complex, Antigen, T-Cell; D016693:Receptors, Antigen, T-Cell, alpha-beta; D016692:Receptors, Antigen, T-Cell, gamma-delta; D011994:Recombinant Proteins