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A Highly Conserved Phenylalanine in the α, β‐T Cell Receptor (TCR) Constant Region Determines the Integrity of TCR/CD3 Complexes
Author(s) -
CASPARBAUGUIL S.,
ARNAUD J.,
HUCHENQ A.,
HEIN W. R.,
GEISLER C.,
RUBIN B.
Publication year - 1994
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1994.tb03469.x
Subject(s) - t cell receptor , avidity , cd3 , biology , microbiology and biotechnology , tyrosine , chemistry , cd8 , stereochemistry , t cell , biochemistry , antibody , antigen , immune system , genetics
In the present study, we have investigated the importance of a phenylalanine (phe 195 ) in the Tcr‐Cα region on Tcr‐α, β/CD3 membrane expression. An exchange of phe 195 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‐α, β/CD3‐γɛ, δɛ complexes and ζ 2 homodimers. The Tcr‐Cα region around phe 195 seems together with the same region in the Tcr‐Cβ region to constitute an interaction site for ζ 2 homodimers. The presence of phe 195 on both Tcr‐Cα and Tcr‐Cβ causes high avidity interaction with ζ 2 homodimers, whereas his 195 in both Tcr‐Cγ and Tcr‐Cδ results in an apparently lower avidity interaction with ζ 2 homodimers. It is suggested that the phe 195 region (on β‐strand F) and eventually adjacent aromatic amino acid residues on β‐strand B region may play an important role in Tcr‐α, β/CD3 membrane expression, in Tcr‐α, β/CD3 competition with Tcr‐γ, δ/CD3 complexes for ζ 2 homodimers and in the control of formation of ‘mixed’ Tcr heterodimers.