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.

Share

COinS