TY - JOUR

T1 - A highly conserved phenylalanine in the alpha, beta-T cell receptor (TCR) constant region determines the integrity of TCR/CD3 complexes

AU - Caspar-Bauguil, S

AU - Arnaud, J

AU - Huchenq, A

AU - Hein, W R

AU - Geisler, C

AU - Rubin, B

N1 - Keywords: Amino Acid Sequence; Animals; Antigens, CD3; Base Sequence; Cell Line; Cell Membrane; Conserved Sequence; DNA, Complementary; Evolution; Humans; Molecular Sequence Data; Phenylalanine; Point Mutation; Protein Conformation; Receptors, Antigen, T-Cell, alpha-beta; Receptors, Antigen, T-Cell, gamma-delta; Sequence Homology, Amino Acid; Sheep; T-Lymphocytes; Transfection; Tumor Cells, Cultured

PY - 1994

Y1 - 1994

N2 - In the present study, we have investigated the importance of a phenylalanine (phe195) in the Tcr-C alpha region on Tcr-alpha,beta/CD3 membrane expression. An exchange of phe195 with a tyrosine residue does not affect Tcr/CD3 membrane expression; however, exchange with aspartic acid, histidine or valine prohibit completely Tcr/CD3 membrane expression. This seems to be due to a lack of interaction between mutated Tcr-alpha,beta/CD3-gamma epsilon,delta epsilon complexes and zeta 2 homodimers. The Tcr-C alpha region around phe195 seems together with the same region in the Tcr-C beta region to constitute an interaction site for zeta 2 homodimers. The presence of phe195 on both Tcr-C alpha and Tcr-C beta causes high avidity interaction with zeta 2 homodimers, whereas his195 in both Tcr-C gamma and Tcr-C delta results in an apparently lower avidity interaction with zeta 2 homodimers. It is suggested that the phe195 region (on beta-strand F) and eventually adjacent aromatic amino acid residues on beta-strand B region may play an important role in Tcr-alpha,beta/CD3 membrane expression, in Tcr-alpha,beta/CD3 competition with Tcr-gamma,delta/CD3 complexes for zeta 2 homodimers and in the control of formation of 'mixed' Tcr heterodimers.

AB - In the present study, we have investigated the importance of a phenylalanine (phe195) in the Tcr-C alpha region on Tcr-alpha,beta/CD3 membrane expression. An exchange of phe195 with a tyrosine residue does not affect Tcr/CD3 membrane expression; however, exchange with aspartic acid, histidine or valine prohibit completely Tcr/CD3 membrane expression. This seems to be due to a lack of interaction between mutated Tcr-alpha,beta/CD3-gamma epsilon,delta epsilon complexes and zeta 2 homodimers. The Tcr-C alpha region around phe195 seems together with the same region in the Tcr-C beta region to constitute an interaction site for zeta 2 homodimers. The presence of phe195 on both Tcr-C alpha and Tcr-C beta causes high avidity interaction with zeta 2 homodimers, whereas his195 in both Tcr-C gamma and Tcr-C delta results in an apparently lower avidity interaction with zeta 2 homodimers. It is suggested that the phe195 region (on beta-strand F) and eventually adjacent aromatic amino acid residues on beta-strand B region may play an important role in Tcr-alpha,beta/CD3 membrane expression, in Tcr-alpha,beta/CD3 competition with Tcr-gamma,delta/CD3 complexes for zeta 2 homodimers and in the control of formation of 'mixed' Tcr heterodimers.

M3 - Journal article

C2 - 8091132

VL - 40

SP - 323

EP - 336

JO - Scandinavian Journal of Immunology, Supplement

JF - Scandinavian Journal of Immunology, Supplement

SN - 0301-6323

IS - 3

ER -