Role of the CDR1 of the TCR β chain in the binding to a MHC-peptide complex
ORCiD
David M. Ojcius: 0000-0003-1461-4495
Department
Biomedical Sciences
Document Type
Article
Publication Title
International Immunology
ISSN
0953-8178
Volume
6
Issue
10
DOI
10.1093/intimm/6.10.1561
First Page
1561
Last Page
1565
Publication Date
10-1-1994
Abstract
Single alanine substitutions were introduced into the CDR1 region of the β chain of a Kd-restricted TCR. Mutants and wild-type TCR were attached to the ζ chain of the CD3 complex and expressed at the surface of a rat basophil cell line. Transfectants were tested for the binding of purified soluble Kd-peptlde complexes. With this experimental system, accessory molecules are unlikely to play a major role and the contribution of each residue to the interaction can be addressed. Results show that all positions in the CDR1 region are involved in the binding to the Kd-peptide complex but at varying degrees. These effects are discussed in relation to a molecular model of the TCR. Comparison of these results with previous data obtained in a T cell hybridoma system suggests the existence of a threshold in the TCR affinity necessary for mature T cell activation.
Recommended Citation
Lone, Y.,
Bellio, M.,
Prochnicka-Chalufour, A.,
Ojcius, D. M.,
Boissel, N.,
Ottenhoff, T. H.,
Klausner, R. D.,
Abastado, J.,
&
Kourilsky, P.
(1994).
Role of the CDR1 of the TCR β chain in the binding to a MHC-peptide complex.
International Immunology, 6(10), 1561–1565.
DOI: 10.1093/intimm/6.10.1561
https://scholarlycommons.pacific.edu/dugoni-facarticles/49