Biophysical and structural studies of TCRs and ligands: Implications for T cell signaling
Biophysical and structural studies of TCRs and ligands: Implications for T cell signaling
The availability of soluble αβ 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 α and β chains have finally established their structural similarity with the Ig 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.
97-106
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Qadri, Ayub
c31c2ac2-aaa5-4236-907c-a96dfbc598e8
February 1997
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Qadri, Ayub
c31c2ac2-aaa5-4236-907c-a96dfbc598e8
Ward, E. Sally and Qadri, Ayub
(1997)
Biophysical and structural studies of TCRs and ligands: Implications for T cell signaling.
Current Opinion in Immunology, 9 (1), .
(doi:10.1016/S0952-7915(97)80165-3).
Abstract
The availability of soluble αβ 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 α and β chains have finally established their structural similarity with the Ig 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.
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Published date: February 1997
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Local EPrints ID: 425119
URI: http://eprints.soton.ac.uk/id/eprint/425119
ISSN: 0952-7915
PURE UUID: c0fca955-c4a9-4f12-aa11-4f4ddfc71ce5
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Date deposited: 11 Oct 2018 16:30
Last modified: 16 Mar 2024 04:37
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Author:
Ayub Qadri
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